VOLUME 1 Chemistry - daviddolphin.comchemistry, biochemistry, and medicine relating to B J2. Volum e 1 emphasizes chem-istry, biosynthesis, history, and nomenclature; Volume 2 covers

Bl2 VOLUME 1 Chemistry

Edited by

DAVID DOLPHIN Department of Chemistry University of British Columbia

1807 ML/1982

A WILEY-INTERSCIENCE PUBLICATION

JOHN WILEY & SONS New York • Chichester • Brisbane • Toronto • Singapore

Contents

1 History of Vitamin B12: Pernicious Anemia to Crystalline Cyanocobalamin 1

Karl Folkers

1 100 to 155 Years Ago, 1

2 56 to 100 Years Ago, 2 3 53 Years Ago—The Nobel Prize, 2 4 36 to 53 Years Ago, 3

5 32 Years Ago-Discovery of Crystalline Vitamin B12, 3 References, 15

2 Nomenclature 17

Waldo E. Cohn

3 X-Ray Crystallography of B12 and Cobaloximes 23

Jenny Pickworth Glusker

1 Establishment of the Chemical Formula of Vitamin BI2 and Vitamin Bi2 Coenzyme 24

2 Details of the Structure of Vitamin B12, the Coenzyme, and Their Analogues, 41

3 Effects of Alterations in the Corrinoid System, 69 4 Model Compounds to Give Information on Mechanism, 80

5 Concluding Remarks, 90 Notes Added in Proof, 91 Appendix I Lists of Analyses Described, 92 Appendix II Methods of X-Ray Crystallography and Glossary, 97 References, 102

4 Biosynthesis of the Corrin Macrocycle 107

Alan R. Battersby and Edward McDonald

1 Introduction, 108

2 Identity of the Primary Precursors of Cobyrinic Acid, 111

3 Mechanistic Study of the Methyl Transfer from Methionine, 113

4 Proof That Uro'gen-III Is a Precursor of Cobyrinic Acid, 116

5 Biosynthesis of Uro'gen-III from PBG ,117

6 Steps Beyond Uro'gen-III ,120

7 Structures of the Dimethylated Isobacteriochlorins Related to Vitamin B12, 123

8 Structure of the Mono-C-Methylated Chlorin (Factor I), 130

9 Structures of the Trimethylated Isobacteriochlorins, 132

10 The Methyltransferase Enzyme System, 135

11 Synthesis of Isobacteriochlorins and Dihydroisobacteriochlorins, 135

12 Experiments on the Loss of C-20 from the Precursor Macrocycle During Formation of Cobyrinic Acid, 137

13 Summary of Pathway to Corrins and Future Prospects, 139 References, 141

Biosynthesis of Cobalamin Coenzymes 145

F. M. Huennekens, K. S. Vitols, K. Fujii and D. W. Jacobsen

1 Introduction, 146

2 Biosynthesis of the Nucleotide Loop of Cobalamins: Conversion of Cobyric Acid to Cobalamin, 148

3 Formation of the Car bon—Cobalt Bon d in C obalamin Co enzymes: Conversion of Cob alamins to Ade nosyl- and Meth ylcobalamin, 15 5 References, 164

The Total Synthesis of Vitamin B12 169

Robert V. Stevens

1 Introduction, 169

2 Synthesis of Cyanobromide 1 (Harvard, 1968), 172

3 The Eastern Half (Cambridge and Zurich), 183

4 Coupling of th e Eastern a nd W estern Halves: S ynthesis of Cob yric Ac id (Cambridge and Zurich), 187

5 The Photochemical Path (Zurich), 192

6 Synthesis of Vitamin B12, 197

Reactions of the Corrin Macrocycle 201

Raymond Bonnett

1 Introduction, 202

2 The Corrin Ligand-Basic Structural Considerations, 203

3 Metallation and Demetallation, 210

4 Meso Substitution, 212

5 Oxidative Cleavage, 217

6 Epimerization at 0-Positions, 220

7 Cyclization Reactions, 225 8 Reactions of Peripheral Acylamide Functions, 230

9 Miscellaneous Reactions, 237 References, 240

7 Synthesis of Organocobalt Complexes 245

Kenneth L. Brown

1 Introduction and Scope of This Chapter, 246

2 Practical Aspects, 247

3 Organocobalt Syntheses via Cobalt (I) Reagents, 250

4 Organocobalt Syntheses via Cobalt(II) Reagents, 271

5 Organocobalt Syntheses via Cobalt(III) Reagents, 277

6 Modification of Organic Ligands, 283 References, 286

9 Reactions of Alkyl Ligands Coordinated to Cobalamins and

Cobaloximes 29

H. P. C. Hogenkamp

1 Introduction, 295

2 Homolytic Cleavage of the Carbon—Cobalt Bond, 296

3 Heterolytic Cleavage of the Carbon—Cobalt Bond, 305 References, 319

10 Coordination Chemistry of the B12 Dependent Isomerase Reactions

32

J. M. Pratt

1 Introduction, 326

2 Why Co? 335

3 Steric Effects on the Structures and Equilibria of DBC and Alkylcobalamins, 341

4 Labilization of the Co—C Bond by Steric Distortion, 361

5 Reactions Related to the Enzymatic Isomerase Reactions, 375

6 Summary, 386 References, 388

11 Electronic Spectra of B12 and Related Systems 393

C. Giannotti

1 General Aspects in the Electronic Transition of Corrinoid Co111

Compounds, 394

2 Theoretical Considerations, 396

3 Nature of the Electronic Transitions, 401

4 Effect of Various Parameters on the Position of the Absorption Bands, 407

5 Electronic Absorption Spectra of B12r and B12s, 418

6 Cobaloximes as Models, 419

7 Circular Dichroism (CD); Magnetic Circular Dichroism (MCD), 420 8 Luminescence, 426

References, 427

10 EPR of B12-Dependent Enzyme Reactions and Related Systems

John R. Pilbrow

1 Introduction, 432

2 EPR of Cobalamins and Cobinamides, 433

3 B12 -Dependent Enzyme Reactions, 444

4 Oxygenation of B 12r(Cbl"), 458

5 Conclusion, 459 References, 460

13 The Nuclear Magnetic Resonance Spectroscopy of Cobalamins and Their Derivatives 463

Otto D. Hensens, H. Allen O. Hill, Charlotte E. McClelland, and Robert J. P. Williams

1 Introduction, 464 2 The 1H NMR Spectrum of Adenosylcobalamin, 465

3 13C NMR Assignments of Vitamin B12 Derivatives, 473

4 Structural Information Revealed by NMR Spectroscopy, 482

5 Biosynthetic Studies, 486

6 The 1H NMR Spectra of Co (II) and Co (I) Corrinoids, 486

7 The Electronic Structure of Corrinoids, 487 8 The Cobalamins as Fluxional Molecules, 490 9 The pH Dependence of the 1H NMR Spectra of Cobalamins, 493

10 The Reaction of Cobalamins with Metal Ions, 495

11 Conclusions, 498 References, 498

11 Chemistry and Significance of Vitamin B12 Model Systems 501

Jack Halpern

1 Introduction, 502

2 Some General Comparisons of B12 and Model Compounds, 504 3 Structural and Steric Aspects, 505 4 Acidities of Hydridocobalt Complexes and Cobalt—Hydrogen Bond Dissociation

Energies, 506

5 Cobalt—Carbon Bond Dissociation Energies, 507

6 Redox Chemistry of BJ2 Model Compounds, 513

7 Formation of Cobalt—Carbon Bonds, 517 8 Cleavage of Cobalt—Carbon Bonds, 524

9 Role of Model Systems in the Study of the Mechanisms of B12-Dependent Enzymatic Reactions, 528

10 Concluding Remarks, 535 References, 535

15 Mechanisms of Action of the B12 Coenzyme: Theory and Models 543

Bernard T. Golding

1 Introduction, 544

2 Cleavage of the Co—C Bond of AdoCbl, 544 3 Hydrogen Abstraction, 554

4 Migration of Group X, 555

5 Modeling AdoCbl-Dependent Reactions, 564

6 Conclusions, 577 References, 578

CONTENTS OF VOLUME 2

1 Biological and Medical Aspects of Vitamin B12

William S. Beck

2 Cobalamin Transport in Microorganisms

Clive Bradbeer

3 Instrinsic Factor, Transcobalamin, and Haptocorrin

Ebba Nexǿ and Henrik Olesen

4 Quantitation of Cobalamins in Human

Serum Ebba Nexǿ Henrik Olesen

5 Metal-Free Corrinoids and Metal Insertion

Volker B. Koppenhagen

6 Mechanisms for B12 -Dependent Methyl Transfer

J. M. Wood

7 Acetate Biosynthesis

Lars G. Ljungdahl and Harland G. Wood

8 Amino Mutases

John J. Baker and Thressa C. Stadtman

9 Diol Dehydrase

Tetsuo Toraya and Saburo Fukui

10 Ethanolaminc Ammonia-Lyase

Bernard M. Babior

11 Glutamate Mutase

Robert L. Switzer

12 B12 -Dependent Methionine Biosynthesis

Robert T. Taylor

13 Methylmalonyl-CoA Mutase

Jdnos Retey

14 Cobalamin-Dependent Ribonucleotide Reductases

Raymond L. Blakley

Preface for Volume 1 Volume 1 contain s chapters on the history, nomenclature, and structure determina-tions o f B12 and related systems. The biosynthesis of the corrin macrocycle and co-enzyme B

12 are covered , along with th e total chemical synthesis of the vitamin .

Reactions o f both the corrin ring and the cobalt-carbon bond are discussed and related to the mechanism of action of coenzyme B1 2 . In addition, chapters on vari-ous aspects of spectroscopy including electronic, EPR, and NMR are included.

The final result is an up-to-date and critical review of the areas described above. This treatise provides, for the first time, a complete and comprehensive review of all of the major chemical, biochemical, and medical aspects of vitamin B1 2 .

I wish to tak e thi s opportunity to thank the contributors t o thi s volume for both the scholarshi p of their work and the promptness with which they all met the various deadlines.

DAVID DOLPHIN

Vancouver, British Columbia November 1981

General Preface The vitami n B 1 2 coenzyme and related corrinoids represent the most complex non-polymeric structures foun d i n nature , and in addition they are the onl y known nat-urally occurring organometallic complexes . Their uniqueness and complexity have presented majo r challenges, and will continue so to do for some time to come, in all areas o f the natural and life sciences . Indeed, solutions to B 1 2-related problems pre-sent some of the principal scientific achievements of the past half century ; each decade has recorded a milestone toward s an understanding of the nature and func-tion o f these systems .

In 1926 Minot an d Murphy announced a dietary treatment of pernicious ane -mia, which had previously proved t o be a fatal disease. In 1934 they were awarded the Nobel Prize for their discoveries concerning liver therapy against anemias . I n 1948 Folker' s group i n th e Unite d States and Leste r Smith' s in Great Britain inde-pendently announced the isolation and crystallization of the red antipernicious ane-mia factor now known as vitamin B1 2 . The structure of vitamin B ! 2 was revealed in 1956 by th e X-ray crystallographi c work o f Hodgkin's group an d by the chemical studies o f Todd an d Johnson . I n 1958 Barker isolated and characterized coenzyme B 1 2 , showing that vitami n B 1 2 (cyanocobalamin ) is an antifact generated during its isolation. The structure of the coenzym e wit h its unique cobalt-carbon bond wa s elucidated once mor e b y Hodgki n i n 1961 . The 1960s saw majo r advance s in our understanding o f both the chemistry and enzymology of B 1 2 and it s coenzyme , culminating in the total synthesis of vitamin B 1 2 by Woodward and Eschenmoser in 1976.

Since there are fewer molecule s o f B 1 2 i n a man than there are red blood cells, it i s not surprisin g tha t there is still much to learn about this molecule. This is espe-cially true i n mammal s where the function of Bt 2 i n such low concentrations is still unclear. Furthermore , although there are many enzymatic reactions dependent on coenzyme B1 2 , its mechanism of action is still obscure.

This wor k consists of two volumes and cover s al l o f the major aspect s o f the chemistry, biochemistry, and medicine relating to BJ 2 . Volume 1 emphasizes chem-istry, biosynthesis , history , and nomenclature ; Volum e 2 cover s biochemical and medical aspects .

I wish to thank Dr . Olga Avramovic fo r her assistance, Alan Johnson for intro-ducing me t o B 1 2 , and the late R. B. Woodward for expanding and encouraging my knowledge an d interes t in the subject .

DAVID DOLPHIN

Vancouver, British Columbia November 1981

Author IndexNumbers in boldface are pages on which names/references appear in text. Numbers in parentheses are reference numbers and indicate that the author's work is referred to although his name may not be mentioned in the text. Numbers in italics indicate pages on which complete references are listed.

Aasa, R., 437(11), 461 Abbott, J. C, 252(41), 288, 418(88),

419(88), 430 Abeles, R. H., 65(56), 68(57), 104, 109

(1), 141, 147(11), 156(52), 160(52), 164, 166, 282(188), 283(188), 284 (188), 239, 310(64), 322, 376(93), 377(95), 382(121, 122), 391, 392, 449(27, 30), 450(41), 451(36, 37, 41), 453(41), 454(41), 461, 462, 469(14), 499, 507(31), 527(118,119), 530(31), 536, 539, 540, 545(5, 27), 547(6, 16), 548(11, 16), 550(11, 16), 551(17), 558 (47), 559(47), 578, 579, 580

Abley, P., 255(80), 278(80), 289, 526 (107), 527(107), 538, 539

Ackermann, G., 404(26), 427 Adams, W. W., 85(88), 87(88), 88(88),

105 Adamson, A. W., 406(52), 428 Adin, A., 526(106), 539 Agnes, G., 311(69), 312(69), 322, 527

(110, 112), 539 Ahond, A., 256(74), 264(74), 304(42),

321, 364(83), 391, 404(37), 405(37), 418(31), 428, 511(49), 537

Alcock,N. W., 706(118) Alicino, J. F., 26(10), 102 Allen, R. H., 268(121), 291 Allerhand, A., 473(18), 480(18), 481

(18), 484(30), 491(18), 499 Allingcr, J., 33(33), 33 Alworth, W. L., 110(3), 120(3), 141 Anderson, B. F., 75(68), 105 Anderson, S. N., 269(136), 291, 516

(74), 538

Anh, N. T , 398(15), 400(15), 411(15), 419(15), 427, 556(38), 562(38), 564 (38), 576(38), 579

Anton, D. L., 313(76), 322 Anton, P. L., 486(36), 499 Arigoni, D., 115(17, 20, 22), 116(20),

126(55), 132(55, 59, 70), 142,144, 377(96), 391, 545(4), 558(4, 46), 577 (4), 578, 580

Armarego, W. L. F., 277(172), 292 Armitage, I. A., 115(19), 117(26), 120

(26), 133(19), 142 Armitage, J. B., 230(79), 234(79) Ash, L. B., 33(33), 103 Ashcroft,M. R., 381(118), 392, 568(63),

569(63), 570(63), 580 Assour, J. M., 438(15), 461{\5) Atkins, M. P., 268(125), 291, 381(116),

392, 568(64, 65, 66), 569(64, 65, 66), 570(65), 580

Auh, N. T., 530(131), 540 Awtrey, A., 352(65), 390 Awtrey, A. W., 244(18, 19), 249(18), 271

(18), 283(18), 287

Babior, B. M., 109(1), 141, 147(9), 155 ( 9 ) , 164, 254(66), 289, 282(194), 291, 293, 331(8), 332(8), 367(8), 376(94), 381(120), 388, 391, 392, 423(102), 430, 449(28, 32), 450(32), 451(28, 32), 452(46), 453(32), 457(46), 461, 462, 469(15), 499, 507(30), 529(126), 530 (30, 126), 534(126), 536, 540, 541, 544(la), 555(34), 558(46, 49), 575(82, 83), 576(92), 578, 579, 580, 581, 582

Bachovchin, W. W., 554(30), 555(30), 579

Bacquet, R., 352(65), 390 Bacquet, R. J., 271(148), 292 Bailey, N. A., 279( 175), 292, 336(25), 389 Baker, H. N., 110(3), 120(3), 141 Ballard, D. H., 269(136), 291, 516(74),

538 Baltimore, B. G., 449(31), 461, 571(69),

581 Balzani, V., 406(50), 428 Banks, A. R., 575(87), 581 Banks, R. G. S., 335(14), 373(90), 389, 391 Bannister, J. V., 468(13), 499 Bannister, W. H., 468(13), 499 Bansal, K. M., 573(76), 581 Barchielli, R., 152(26), 154(26), 165 Barker, H. A., 30(31), 54(53), 103,104, 147(1, 2), 152(27), 156(43,47), 159 (43), 164, 165, 296(2), 297(3), 305(44), 306(52), 312(72, 73), 319, 320, 321, 322, 331(9, 10), 353(68), 366(10), 367(91), 388, 390, 418(92), 430, 449 (31), 452(45), 457(45), 461, 462, 571 (69), 581 Barnett, R., 310(64), 322, 527(118, 119),

539 Barrick, J. C, 85(92), 705 Bartczak, T. J., 75(68), 105 Bartels,G., 219(58), 242 Bartlett, M. W., 75(65), 87(100), 88(100),

104, 105, 269(138), 291 Bartosinki, B., 165(41) Battaglia, L. P., 706(110) Battersby, A. R., 111(8), 112(14), 113

(14), 114(18), 115(18), 116(8, 25), 117(25, 28,29,31), 118(28, 29, 33, 35, 36, 37), 120(25b), 121(41), 122 (43, 46), 123(43, 46, 49), 125(43, 46, 51), 126(46,51,53), 127(28a), 128 (46), 129(43,56), 130(56), 132(49, 60), 133(60, 61), 134(61), 135(43, 60, 61, 64, 66), 137(61), 141(69), 142, 143, 144, 218(56), 242, 482(25), 486(37), 499, 500

Batton, P., 281(185), 293 Bayston, J., 458(56), 462 Bayston, J. H., 439(21), 442(21), 443

(21), 444(21), 445(21), 449(21), 461 Bayston, J. N., 277(167), 292 Beavan, G. H., 204(8), 215(8), 240 Beaven,G. H., 41S(9\),430 Beavin, G. H., 277(165), 292

Beck, W. S., 160(65), 166 Becker, W., 37(43, 44), 39(43), 40(47)

104, 229(74), 230(78), 242 Beckham, T. M., 262(103), 263(102),

290, 363(82), 391, 571(70), 581 Beckhans, H-D., 548(10), 578 Beinert,H., 381(120), 392, 449(32), 450

(32, 35), 451(32), 453(32), 455(35, 53) 456(53), 461, 462, 558(49, 50), 580

Beisbarth, H., 231(84), 242 Belford, R. L., 440(23, 24), 461 Belikov, A. B., 298(12), 299(12), 320,

363(81), 391, 573(77), 557 Bendle,S., 527(112), 539 Bercaw, J. E., 515(65), 537 Bergmann, K.-H., 123(47, 48), 125(47,

48), 126(47), 127(47), 128(47), 13o' (47), 132(48), 134(48), 143

Bernhauer, K., 110(2), 120(2), 747, 148 (14), 151(21), 152(24, 28), 164,165, 312(71), 316(87), 322, 323, 417(79), 429, 216(46), 221(63), 226(46), 230 (81, 82), 231(83, 84, 89), 235(91), 236(94, 95), 238(82), 241, 242, 243, 254(67), 278(174), 289, 292

Bertele,E., 236(96), 243 Bidling,G., 87(125), 106 Bidlingmaier, G., 377(101), 392, 533

(146, 147, 148), 540, 564(54), 580 Bieganowski, B. R., 413(72, 73, 74, 75,

76), 415(72), 420(72, 73), 421(72, 73), 429

Bieganowski, R., 92(127), 106 Bigotto, A., 106(107), 256(91), 270(91),

280(91), 290, 336(24), 389, 391, 502 (3), 505(17), 514(3), 531(17), 535, 536

Birke, R. L., 514(60), 522(60), 537 Blach, D. STC, 92(128), 106 Blackburn, R., 318(94, 96, 97), 319(97),

323, 376(91,92), 391 Blackmer, G. L., 258(96), 290 Blakley, R. L., 313(74), 322, 432(2, 3),

433(2, 3), 439(3), 441(3), 442(3), 449 (3, 34, 39), 450(35), 451(39, 40), 453 (39, 40), 455(35, 52, 53, 54, 55), 456 (52, 53, 54), 460, 461, 462, 558(50), 580

Blandhard, H. S., 404(23), 427 Barker, H. A., 432(1), 460 Blaser,H., 273(158), 292 Blaser, H. U., 211(32), 241, 513(59),

520(59), 522(59), 535(59), 537 Blaylock,B. A., 162(72), 166

Boas, J. F., 381(119), 382(119), 392, 438(12a), 452(44), 453(44), 454(44), 457(44), 461, 462, 559(51), 580

Bock, D. L., 260(99), 290 Bogard, T. L., 118(38), 126(54), 143,

144 Bolton, J. R., 404(38), 405(38), 418

(38), 428, 525(94, 95), 538, 539 Bonneau, R., 404(42), 418(42), 419(42),

428 Bonnett, R., 33(39), 103, 110(5), 120 (5), 125(50), 141,143, 153(30), 165, 202(2, 4), 203(4), 204(2), 208(24), 212(12), 215(2, 11), 218(2), 220(2, 11), 221(62), 222(64), 224(24, 64), 225(11), 226(11), 227(11), 229(75), 230(87), 231(87), 233(87), 234(4, 62, 65, 80), 235(62), 236(11, 65), 238(11), 240, 241, 242, 345(60), 390, 417(81), 418(80), 429, 485(33), 499 Boos, R. N., 419(94), 430 Boretti, G., 152(26), 154(26), 165 Borodulina-Shvets, V. I., 267(109), 290 Borodulino-Shvets, V. I., 305(49), 306

(49), 321 Boucly, P., 251(39), 288 Boudy, P., 279(179), 293 Bovmann, D., 212(36), 220(36), 241,

345(61), 390 Bowden, F. L., 329(5), 345(5), 388 Bower, B. K., 125(50), 144 Bowman, J. T., 249(25), 254(24), 278

(25), 287 Bowman, R. L., 426(106), 430 Boxer, G. E., 404(43), 428 Boyle, M. F., 514(60), 522(60), 537 Bozdech, J. ML, 455(52), 456(52), 462 Brady, R. O., 156(43), 159(43), 165, 418

{92),430 Bragg, W. L., 24(2), 102 Braterman, P. S., 340(41), 389 Bray, R .C, 111(10), 142, 218(51), 241, 486(39), 500 Bresciani-Pahor, N., 86(95, 111), 87(112), 105,106, 359(72), 375(72), 382(72), 391, 491(47), 500, 505(18, 19, 20), 506 (20), 531(18, 19, 20), 536 Breslow, R., 261(102), 290, 379(108), 392 Briat, B., 418(86), 426(86, 103), 429, 430 Brink, C, 26(11), 102 Brink, N. G., 25(5), 102, 239(104), 243 Brink-Shoemaker, C, 26(19), 103, 342 (43), 389

Brodie, J. D., 163(78), 166, 255(87), 289, 306(53), 321, 343(58), 344(58), 349(58), 350(58), 354(58), 362(76), 369(76), 390, 391, 426(106), 430, 469(16), 471(17), 486(17), 487(17), 499

Brot, N., 163(79, 84), 167, 254(71), 289

Brown, C. E., 112(12), 142 Brown, D. G., 291(119), 307(59), 322,

430, 432(4), 449(4), 460, 469(15), 486 (35), 499, 504(7, 10), 528(7, 10), 535, 536

Brown, D. L. S., 508(40), 537 Brown, K. L., 248(14, 17, 20, 21, 22),

249(14, 17, 18), 254(72), 256(89), 257(89), 266(89), 270(145), 271(18, 148), 276(145), 278(173), 283(18, 22), 284(17), 287, 289, 292, 302(33), 308 (60, 61, 62), 309(60), 311(67), 314 (11), 321, 322, 352(65), 390, 504(13), 527(117), 529(117), 534(1?5), 536, 539, 575(86, 89), 581, 582

Brown, T. L., 494(49), 496(49), 500 Brownson, C, 449(34), 461 Bruckner, S., 706(106), 343(51), 349(51),

360(51), 390, 505(16), 531(16), 536 Brydon, G. A., 514(60), 522(60), 537 Buchanan, D. H., 254(75), 260(98), 268

(138), 289, 290, 291, 317(88), 323, 523(88), 538

Buchler, J. W., 125(50), 144 Buckel, W., 115(21), 142 Buckman, T., 297(120), 303(36), 321, 405

(45), 428 Bud6-Zahonyi, E., 248(23), 252(23, 47,

50), 253(47, 60, 61), 288 Buettner, G. R., 382(123), 386(124), 392,

451(43), 452(43), 453(43), 454(43), 457(43), 462

Buhler, N., 239(102), 243 Buisson, D. H., 468(12), 499 Bukin, V., 121(42), 122(42, 43), 125

(45), 129(43), 135(43), 143 Buley, A. L., 532(135), 534(135), 540 Bunn,C. W., 106(122) Burgi, H. B., 398(15), 400(15), 411(15),

419(15), 427, 530(13), 540, 556(38), 562(38), 564(38), 576(38), 579

Burke, G. T., 163(78), 766 Burnett, M. G., 252(49), 288 Burnham, B. F., 479(22), 484(22), 487

(22), 499 Burton, G., 118(34), 143

Bury, A., 381(118), 392, 568(63, 66), 569(63, 66, 67) , 570(63), 580, 581

Busch, D. H., 250(33, 34), 287, 288, 404(35), 418(35), 42*

Bushell, M. J., 144(11) Bykhovsky, V., 122(43), 123(43), 125

(43), 129(43), 135(43), 143 Bykhovsky, V. Ya., 121(42), 122(42),

125(51), 126(51), 143, 144

Cacevar,C, 526(109), 539 Cagen, L. M., 157(58), 166 Calderazzo, F., 254(64), 289, 335(20), 389 Calligaris,M., 86(95, 111), 87(112), 105,

106, 343(51), 349(51), 359(72), 360 (51), 375(72), 382(72), 390, 391, 491 (47), 500, 505(16, 18, 19), 531(16, 18, 19), 536

Callot, H. J., 280(183, 184), 281(183, 184), 293

Cambridge group, 135(65), 144 Candlin, J.?., 428 Cannon, A. W., 230(79), 234(79, 80),

242 Cannon, J., 27 Cannon, J. R., 110(5), 120(5), 141, 202

(2), 204(2, 11), 215(2, 11), 218(2, 50), 220(2, 11), 225(11), 226(11), 227(11), 231(11), 236(11), 238(11), 240, 241, 417(81), 418(80), 429

Cantoni,G. L., 156(46), 165 Carassiti, V., 406(50), 428 Cardin, D. J., 299(13), 320 Carr, J. E., 419(94), 430 Carr, S.G., 453(50), 462 Carrell,H. L., 24(1), 102, 106 Carry, T. J., 282(188), 283(188), 284

(188), 293 Cason,J.,33(33),70J Cass, A. E. G., 468(13), 499 Castanera, E. G., 156(43), 159(43), 165 Castro, C. E., 522(86), 538 Caughlin, C. N., 404(25), 427 Cesari,M., 280(182), 293 Chan, M. S., 515(70), 516(70), 535(70),

538 Chanser, E. G., 298(8), 320, 363(80),

391 Chao, T.-H., 252(45), 253(59), 269(135),

288, 291, 507(27), 536 Charbonneau, L., 490(50), 495(50), 497

(50), 500

Charton, M., 256(85), 271(85), 289 Chaston, S. H. H., 438(12b), 461 Chatt, J , 340(39), 389 Cheh, A., 539 Chemaly,S., 567(61), 580 Chemaly, S. M. , 343 (54), 344(54), 351

(54), 352(54), 353(54), 355(54), 357 (54), 358(54), 359(54), 360(54), 362 (54, 78) , 364(54), 365(54, 86) , 366 (54), 368(54), 371(54), 376(54), 379 (78), 380(86), 390, 391

Cheney, B. V., 130(58), 144 Chernoff, D., 248(21), 287 Chervyakova, T. G., 282(189, 190), 284

(199, 201, 202, 203), 285(202), 293, 294, 549(14), 575(85), 578, 581

Cheung, A., 469(14), 499 Chin, C. A., 422(101), 426(101), 430 Chock, P. B., 273(155), 292, 352(65),

390, 511(48), 518(48), 519(48), 535 (48), 537

Chrzastowski, I. Z., 516(74), 538 Chrzastowski, J. Z., 525(100), 526(100),

539 Chu,M. M. L., 575(89), 582 Chung, S. K., 379( 107), 392, 532( 145),540 Cioffari, A., 556(44), 580 Clark, V. M„ 110 (5), 120(5), 141, 204

(11), 215(11), 218(55), 220(11, 55) , 225(11), 226(11), 227(11), 231(11), 236(11), 240, 242, 418(80), 429

Clarke, D. A ., 246(3), 252(3), 266(3), 277(3), 286, 302(32), 321, 335(19), 389

Clauser,S. C, 412(66), 429 Cocevar,C, 525(99), 539 Cockle, S. A., 353(66, 67), 390, 430,

439(206), 451(38), 452(38), 456(6), 458(57), 461, 462, 468(11), 469(11), 498, 499, 558(48), 580

Coffman, R. E., 382(123), 386(124), 392, 451(40, 43), 452(43), 453(43), 454(43), 455(53, 54), 456(53, 54), 457(43), 462

Coleman, W. M., 252(40), 288 Collar, J. W., 252(41), 254(41), 288, 418

(88), 419(88), Conn, J. B., 419(94), 430 Connolly, P. J., 252(49), 288 Connor, J. A., 508(40), 537 Cooksey, C. J., 266(108), 267(108), 285

(205), 286(205), 290, 294, 525(100), 526(100), 539, 569(67), 581

Cooper, N. J. , 5 30(132), 540, 547(8), 559(8), 576(8), 578

Cooper, N. John, 452(49), 462 Corcoran, J. W., 111(9), 142 Corey, E. J. , 45 2(49), 462, 530(132),

540, 547(8), 559(8), 576(8), 578 Cornforth, J. W., 115(21), 142 Corradi, A. B., 706(110) Costa, G., 250(35), 254(63, 65), 256

(91), 270(91, 143), 271(143, 146), 277(170, 171), 280(91), 288, 289, 290, 291, 292, 301(28), 317(90), 320, 323, 336(24), 389, 490(45), 500, 502(3, 4), 504(4), 514(3, 4, 61, 62, 63), 525(99), 526(109), 535, 537,539

Coulter, C. L., 35(48), 103, 154(36), 165, 342(45), 389

Cox, D. L., 318(94), 323 Craig, P. J., 330(6), 335(6), 338(30),

349(6), 361(6), 364(6), 366(6), 367(6), 388, 389, 419(97), 430, 504(9), 508 (9), 536

Cram, D. J., 547(9), 548(9), 578 Crosby, G. A., 406(57), 428 Cross, R.J.,340(41), 389 Crowfoot-Hodgkin, D., 75(66), 104 Cruichshank, D. W. J., 26(19), 103, 342 (43), 389 Crumbliss, A. L., 249( 24, 25) , 2 54(24),

268( 132, 133), 278(24, 25), 287, 291 CuUen, W. R., 575(87), 581 Cummins, D., 279(176,177), 282(177), 293 Currie, M., 78(74), 105 Cushley, R. J ., 112(13), 113( 16), 142,

473(19), 479( 19), 480( 19), 481( 19), 499

Cutler, A. R., 575(87), 581

Dale, D., 33( 36, 37) , 103, 205(15), 207 (15), 240, 342(47), 344( 47), 3 47(47), 390

Dalling, D. K. , 480(23), 48 1(23), 488 (23), 499

Dalton, D. , 379( 107), 392, 532( 145) , 540

Danon, J , 338(35), 389 Das, P. K., 252(44), 288 Dauner, H.-O., 117(27, 30), 142 Davaquet, A , 530(131), 540 Davidson, A , 438(16), 461 Davies, M. T., 352(64), 365(64), 390 Davies, S. P., 451(38), 452(38), 462, 558 (48), 580

Davis, J. A., 92(128), 106 Day, P., 396(5, 6), 397(5, 6), 398(5, 6),

401(5), 403(5), 409(5, 6), 427, 487 (41), 500

DeBolfo, J. A., 462(59) Deeg, R., 123(47, 48), 125(47, 48), 126

(47), 127(47), 128(47), 129(57), 130 (47), 132(48, 57, 59), 134(48, 57), 135(57), 137(57), 143, 144

Demon, P., 115(19), 133(19), 142 Deniau, J., 512(56), 525(56), 537 Deppish,B., 87(125), 106 Derynck, J., 251(39), 279(179), 288,

293 deSavorgnani, E., 271(146), 292 DeSimone, R. E., 490(50), 495(50), 497 (50), 500 Deutsch, E., 85(91, 94), 105, 158(61),

166, 250(30, 31), 253(30), 254(31), 258(31), 287, 391

Devaquet, A., 398(15), 400(15), 411(15), 419(15), 427, 556(38), 562(38), 564 (38), 576(38), 579

De Vries, B., 507(26), 536 Dewar, M. J. S., 567(60), 580 Dicker, I. D., 243(100) Diehl, H., 418(87), 430 Diehl, N., 239(103), 243 DiGirolamo, P. M., 163(82), 167, 300(16)

320 Dilworth, M. J., 529(124, 125), 540 Dimarco, A., 110(2), 120(2), 141, 152(26

154(26), 765 Dimsdale, M. J., 229(75), 242 Dizikes, L.,559 Dizikes, L. J . , 539 Djerassi, C, 418(86), 426(86, 103), 429,

430 Doak,G. O., 340(38), 389 Doblcr, M., 77(71), 78(71), 105 Dockal, E. R., 255(80), 278(80), 289, 526(107), 527(107), 538, 539 Dodd, D., 246(2), 256(2, 93), 257(93), 261(93), 263(93), 265(93), 266(108), 267(108), 268(134), 277(166), 285 (204, 205), 286(204, 205), 286, 290, 291, 294, 330(7), 335(7), 364(7), 365

(7) , 367(7), 388, 504(8), 516(74), 517 (8) , 525( 101), 527( 101), 536, 53 8, 539 551(18), 579

Doddrell, D., 473(18), 480(18), 481(18), 484(30), 491(18), 499

Dodson, E., 91(126), 106

Eckert, R., 402(21), 403(21), 420(21), 427 Ecoles, T. K., 78(77), 105 Edelev, M. G., 282(189), 284(199, 202

203), 285(202), 293, 294, 549(14), 575(85), 578, 581

Edelhansen, J. H., 404(44), 428 Edelstein, N., 438(16), 461, 466 Edmond, E., 33(38, 39), 103, 208(24),

223(67), 224(24, 67), 241, 242, 342 (46), 345(60), 390

Edmond, E. D., 75(66), 104, 706(120) 207(20), 240, 342(50), 390

Eggerer,H., 115(21),742, 532(139,140),540 Eisenstein, O., 398(15), 400(15), 411(15)

419(15), 427, 530(131), 540, 556(38), ' 562(38), 564(38), 576(38), 579

Eisner, U., 125(50), 143 Elder, L. G., 85(84), 105 Elder, R. C, 85(86, 89, 90, 91, 92, 93, 94),

102(86), 105 Elkin,M.,3(l),4(l),75 Elliot, D. F., 235(92), 243 Ellis, B., 26(9), 102, 204(8), 215(8), 240 Ellis, P. E., Jr., 85(93), 105 Elroi,H„ 574(81), 581 Elsenhaus, B., 72(61), 104, 211(30), 247 Elson,C. M., 281(185), 293 Elvoi, H., 292(151) Endicott, J. F., 246(6), 271(6, 149), 272

(149), 287, 292, 299(14), 300(23), 320, 335(13), 336(23), 363(23, 79), 373(23), 376(23, 79), 389, 391, 404(40, 41), 405 (40, 41), 418(40, 41), 428, 503(5), 508 (5, 41), 511(46), 524(5), 525(5, 46), 535, 537,553(25), 554(28), 579

Engel, J., 137(68), 744 Epps, L. A., 85(85), 86(85), 105 Erkol, A. Y., 318(96), 323, 376(91), 391 Ernst, L., 37(43), 39(43), 104, 218(58, 59),

229(74), 242 Ershova,T. E., 298(12), 299(12), 320, 363

(81), 391,513(11), 581 Eschenmoser, A., 75(75), 78(75), 105, 113

(15), 126(54), 135(66), 136(67),742, 744, 202(5),204(14),207(14),209(5), 211(22), 212(5, 33, 36), 213(40), 214(5), 217(5), 220(36), 227(5), 230(5), 236(96), 239 (102), 240, 241, 243, 345(61), 390

Espenson, J. H., 252(45), 253(58, 59), 260 (100), 269(135), 272(150), 277(150), 288, 290, 291, 292, 507(27), 525(97, 98), 526(106), 536, 539, 575(90), 582

Essenberg, M. K., 449(30), 467, 545(2), 578

Dolphin, D., 109(1), 747, 147(11), 764, 216(43, 45), 241, 246(3), 247(11), 248 (15, 16), 249(11), 251(11), 252(3), 254 (11), 257(11), 266(3), 277(3), 281(15, 16, 187), 282(15, 16, 187, 188, 194), 283(187, 188,195, 196, 197), 284(188, 197), 286, 287, 293, 302(29, 32), 306 (54) , 315( 79, 80, 8 1, 82, 83) , 316( 82, 83), 318(54), 321, 322, 323, 376(93), 391, 418(89), 419(89), 429, 430, 449 (27), 461, 507(31), 508(34), 524(34), 530(31), 534(152, 154, 156), 536, 538, 541, 547(16), 548(16), 550(16), 575(87), 578, 581

Dove, M. F., 110(3), 120(3), 141 Dowd, P., 377(98, 99, 100, 103), 379(99),

392, 532(142, 143), 540, 564(55), 565 (55) , 566(55), 567(62), 571(68), 580, 581

Dreos, R., 317(90), 323 Dresow, B , 37(41), 40(47), 74(41), 104 Drevs, H., 335(18), 5S9 Drexhage, K. H., 396(2),398(2),401(2),427 Dubs, P., 113(15), 142 Duc-Hiep,T„ 335(18), 389 Duetsch,E , 523(87), 538 Duggan, D. F., 426(106), 430 Dunham, W. R., 382(122), 392, 450(41),

451 (41), 453(41), 454(41), 462, 558(47), 559(47), 580

Dunhill, R. H., 438(12a), 461 Dunitz, J. D., 75(62, 63, 64, 65), 77(71),

78(62, 64, 71, 74, 76), 80(62), 87(100), 88(100), 704, 105, 106, 241, 269(138), 291

Dunne, C. P., 247(12), 249(1 2), 251(12), 254(12), 257(12), 287

Duong, K. N. V., 253(53), 256(53, 74, 92, 93), 257(53, 92, 93), 260(92), 267(92, 93), 263(53, 92, 93), 264(74), 265(53, 93), 288, 289, 290, 300(18), 304(42), 320, 321, 364(83), 391, 404(37), 405 (37), 418(37), 428, 511(49), 512(54, 55), 524(90), 525(54, 55), 537, 538

Durell, J., 156(46), 765 Dwek, R. A., 464(1), 467(1), 471(1),

491(1), 498

Eager, R. G., 449(31), 467, 571(69), 581 Eaton, D. R., 379(115), 392 Ebnbthcv, A., 204(9), 240 Eckert, H., 255(76), 261(76), 289, 523 ( S I ) , 538

Esscnberg, M. R., 377(95), 391 Evans, H., 33(39), 103, 208(24), 224 (24), 241, 345(60), 390

Eagerness, P. E., 118(4), 143 Fanchiang, Y. T., 517(76), 538 Fantes,K.H., 25(7), 102 Farmery, K., 250(34), 288 Farooq,S., 212(33), 241 Farragi,M., 318(95),323 Fee, J. A., 382( 122), 392, 450(41), 451

(36, 41) , 453( 41), 454( 41), 462, 558 (47), 559(47), 580

Feller, B. A , 40(46), 104 Felner, I., 247(39) Fendler, J. H., 409(62), 429 Fenton, W. A., 156(55), 157(56), 166 Ferraudi, G. J., 300(23), 320, 336(23),

363(23), 373(23), 376(23), 389, 404 (41), 405(41), 418(41), 428, 511(46), 525(46),537, 553(25), 579

Finkbeiner, H. L., 404(23), 427 Finke, R. G., 547(150) Finlay, T. H., 68(57), 104, 461(29),

545(5), 578 Firth, R. A., 255(81), 289, 336(27),

343(52), 346(52), 347(52), 348(52), 349(52), 350(52), 351(52), 354(52), 362(52), 369(52), 389, 390, 394(1), 395(1), 397(8), 404(28), 407(1), 408(8), 409(1, 8), 412(67), 420(1), 422( 1), 427, 429, 468( 10), 482(29), 484(29), 487(29), 488(29), 490(29), 491(29), 499

Fischli, A., 75(75), 204(14), 207(14), 212 (36), 220(36), 240, 241(39), 345(61), 390, 427

Flohr, H., 87(99), 88(99), 705, 269(139), 270(141, 142),297, 377(101), 379 (104, 106), 392, 533(146, 147, 148), 540, 564(54), 565(57), 580 Florian, L. R., 85(90), 105 Floriani, C, 254(64), 289, 335(20), 389 Folkers, K., 25(5), 26(8), 102, 110(6),

747, 2 18(53), 2 39(104), 2 47, 243 Fontaine, C., 404(36), 405(36), 406

(36), 418(36), 419(36), 428, 512 (53, 54, 55), 525(53, 54, 55), 537

Fookes, C. J. R., 117(28, 32, 33), 118 (28, 33, 35, 3 6, 37) , 127( 28a), 742, 143

Ford,S.H.,110(4),747,150(17),151(17),764

Forster, L. S., 406(53), 428 Foster, M. A., 451(38), 452(38), 462, 558

(48), 580 Foster, T., 573(79), 581 Fox, J. P., 398(11), 427 Francia, M. D., 312(70), 322, 539 Frey, P. A., 377(95), 391, 449(30), 461, 545, 578 Frick, T„ 312(70), 322, 539 Friedlina, R. G., 556(42), 580 Friedman, S., 147(5), 164, 529(124, 125), 540 Friedmann, H. C., 110(4), 747, 148(12, 13), 150(17), 151(13, 17), 153(31, 32, 33), 154(36, 37,40), 155(40), 157(58), 764, 765, 766 | Friedrich, W., 92(127), 106, 110(2), 120 (2), 747, 152(24), 161(71), 765, 766, 221(63), 231(85), 236(94, 95), 242, 243, 249(27), 267(116), 257, 290, 301(26, 27), 320, 413(72, 73, 74, 75, 76), 415 (72), 420(72, 73), 421(72, 73), 429 Fritz, H. L., 260(100), 290, 539 Fuendes, R., 268(126), 297, 482(24), 487(24), 488(24), 489(24), 493(24), 497(24), 499 Fugate, R D., 422(101), 426(101), 430 Fuhrer, W., 202(5), 209(5), 210(26), 212 (5), 214(5), 217(5), 227(5), 230(5), 240, 241 Fujii, K., 162(75, 76, 77), 163(82), 766,

767 Fujii, Y., 295(181) Fukui, S., 253(57), 288, 301(25), 302

(30), 306(51), 311(65), 320, 321, 322, 508(38), 522(84), 524(38), 525(38), 536, 538

Funabiki, T., 569(67), 581 Fung, M.M., 397(9), 427 Fyfe,J. A., 153(33), 765

Gakenheimer, W. C, 40(46), 104 Gale, I. A. D., 125(50), 143, 204(13), 240 Galivan, J.H., 162(76), 766 Gams, R. A., 156(54), 766 Garbers, C. F., 247(49) Gardiner, D. J., 344(55), 390, 398(10), 427 Garstki,C., 765(34) Gastaldo, C., 33(33), 703 Gatford, C., 266(108), 267(108), 290

Gould, D. C, 449(28), 451(28), 467 Graf, F., 441(25), 442(25), 467 Grant, D. M., 130(58), 744, 477(20), 480

(23) , 481(23), 488(23), 492(20), 499 Grant, M. E., 268(126), 297, 306(56),

522, 482(24), 487(24), 488(24), 489 (24) , 493(24), 497(24), 499

Grate, J. H., 297(5), 307(5), 320, 351(62) 355(62), 357(62), 358(62), 362(62), 364 (62), 367(62), 368(62), 369(62), 370(62) 371(62), 390, 511(50), 557, 552(21), 553 (21),579

Gratzel, M., 573(76), 581 Greaves, M. L., 35(40), 103, 342(45), 389 Green, M. L. H., 335( 17), 340( 17), 389,

452(49), 462, 530(132), 540,547(8), 559(87), 576(8), 578

Griffith, J. S., 438(13), 467 Griffith, W. P., 276(160), 292 Grigg, R , 77(70), 105, 203(6), 240, 243,

246(3), 252(3), 266(3), 277(3), 286, 302 (32), 527, 335(19), 340(37), 389

Gross, G., 236(95), 245 Gruning, B., 37(43, 45), 39(43), 104, 229

(74, 76, 77), 236(98), 242, 245, 485(31), 499

Gschwend, H., 236(96), 245 Guest, J. R., 147(5), 764, 529(124,125),540 Gunter, J. B , 554(30), 555(30), 579 Gunter, J. D., 426(105), 430 GUnthard, Hs. H., 441(25), 442(25, 26),

458(60), 459(60), 467, 462 Gunzer,G., 117(30), 129(57), 132(57),

134(57), 135(57), 137(57), 742, 744 Gupta, R. K., 485(34), 499, 569(67), 581 Gurevich, V. M., 305(50), 306(50), 527 Guseva, A. S., 267(110), 290, 305(50),

306(50), 527 Gustafson-Potter, K. E., 118(35, 36), 745 Gutschow,C., 115(21), 742

Halpern, J., 253(54), 255(80), 264(105), 273(152, 153, 154, 155, 156, 157, 158), 275(156, 157), 278(80), 288, 289, 290, 292, 335(16), 377(97), 385(97), 389, 391, 428, 502(1), 504(11), 506(23), 507 (29), 508(42), 510(42, 45), 511(42, 47, 48), 512(51, 52), 513(59), 514(23), 515 (65, 70), 516(70, 73), 517(69, 75), 518 (22, 47, 48), 519(22, 48), 520(59), 522 (59), 526(1, 107), 527(107), 529(1), 530 (42), 531(11), 555(1, 11, 22, 42, 48, 59, 70), 556, 537,538, 539

Gaudemer, A., 251(39), 253(53), 256 (53 74, 92, 93), 257(53, 92, 93), 260 (92), 261(92, 93), 263(53, 92, 93), 264 (74)', 265(53, 93), 279(179), 288, 289, 290, 293, 300(18), 304(42), 320, 321, 364(83), 391, 404(37), 405(37), 418 (37), 428, 511(49), 512(53, 54, 55, 56), 525(53, 54, 55, 56), 524(90), 537, 538

Gaus, P. L., 249(24, 25), 254(24), 268 (132, 133), 278, 291

George, P., 412(66), 429 Georgopapadakou, N., 117(26), 120(26),

142 Ghambeer, R. K., 449(34), 461 Giannotti, C, 404(36, 38, 39, 42), 405(36, 38, 39), 406(36), 418 (36, 38, 39, 42), 419(36, 39, 42), 428, 512(53, 54), 525(53, 54, 94, 95), 537,538, 539, 553(23), 579 Gibson, J. F., 467(14) Gilbert, B.C., 573(75), 557 Gill, J., 527(38), 524(92), 538 Glusker,D. L., 33(33), 103 Glusker, J. P , 28(23), 47(51), 103,104,

706(121), 504(12), 536 Gneuss, K. D., 123(48), 125(48), 129(57),

132(48, 57), 133(62), 134(48, 57, 62), 135(57, 62), 13 7(57, 62) , 143,144

Godfrey, J. M., 33(39), 103, 208(24), 221(62), 224(24), 234(62, 65), 235 (62), 236(65), 247, 242, 345(60), 390, 485(33), 499

Goedken, V. L., 275(159), 292, 335(21), 389

Goh, L. Y., 515(65), 537 Golding, B. T., 112(4), 113(14), 114(146),

742, 218(56), 242, 268(125), 281(116, 117), 282(192, 193), 284(192, 198), 297, 292, 293, 303(39), 316(39), 527, 452(47, 48), 462, 482(25), 499, 504(15), 507(32), 508(32, 39), 525(39), 528(32), 529(32), 530(32), 532(136, 137, 138), 534(136, 149), 556, 557, 540, 549 (If, 14), 547, 553(24), 556(36), 557(36), 558(le, 36), 559(36), 568(64, 65, 66), 569(64, 65, 66), 570(65), 571(69, 73), 572(74), 573(36), 575(73, 75, 84), 578, 579, 580, 581

Gossauer, A., 37(43, 45), 39(43), 103, 137 (68), 744, 216(47), 219(59), 228(47), 229(74, 76), 236(98), 247, 242, 245, 485(31), 499

Hamilton, A., 161(68), 766 Hamilton, A. L., 238(99), 245, 281(185), 293 Hamilton, J. A., 432( 2, 3) , 433( 2, 3) , 439

(3), 441( 3), 442( 3), 449( 3, 39, 4 0), 451 (39, 40), 453(39, 40), 460, 462

Hamilton, R., 576(93), 582 Hamm, D. J., 426(105), 430 Hanaucr, R., 125(50), 143 Hanna, M . L. , 527(38), 40 4(32), 405( 32),

418(32), 425, 524(92), 538 Hansen, H. J., 556(43), 580 Hanson, J., 538(61) Hanson, K. R., 562(52), 580 Hanzlik, J., 252(48), 288, 335(15), 388 Hardeggev, B , 212(33), 247 Harris, D. L., 153(31), 165 Harris, R. K., 477(20), 492(20), 499 Harrison, H. R., 75(67), 104 Harrison, M. J., 27 Harrod, J. F., 404(24), 427 Harrowfield, B. V., 439(19), 440(24), 467 Hart, A. C, 156(53), 766 Hartshorn, A. J. , 92( 128), 106, 267(115),

290, 298(11), 320, 573(78), 557 Hasemann, V., 468(13), 499 Hashimoto, N., 213(40), 247 Haslinger, E., 126(53), 744 Hastings, A. B., 3(1), 4(1), 75 Hausinger, R., 495(51), 497(51), 500 Hawkinson, S. W., 35( 40), 103, 154(36),

765, 342(45),390 Hayon,E., 250(32), 257 Hayward, G. C, 314(78), 322,412(71),42P Heeg, M. J., 85(86, 91, 94), 102(86), 105 Heger, I., 117(30), 742 Heise, K. P. , 216( 47), 219( 59), 228(47),

247, 242 Helgeland, K., 228(72), 242 Hellmann, G., 548(10), 575 Henderson, R. J., 373(90), 391 Henglein, A., 573(76), 557 Henry, R. A., 706(118) Hensens, O. D., 353( 67), 390, 456(5, 6) ,

467(5, 7) , 4 68(7), 469( 7), 471( 7), 472 (7), 473( 5, 7) , 482( 7), 483( 7), 484(7), 492(7), 493(7), 494(7), 496(5), 495

Herbst, M. M., 449(31), 467, 571(69), 557 Hesse, D , 404(26), 427 Hester, R. E., 344(55), 390, 398(10), 427 Hicks, P. R., 381(119), 382(119), 392, 452

(44), 453(44), 454(44), 457(44), 462, 559(51), 580

Higson, B. M., 279(175, 176), 282(177), 292, 293, 336(25), 559

Hill, E. A., 379(114), 592 Hill,H. A. O., 255(81, 82), 259, 311(69),

312(69), 522, 336(27), 343(52, 59), 345 (59), 346(52), 347(52), 348(52), 349(52), 350(52),351(52),353(59,66,67),354(52), 361(75), 362(52), 369(52), 389, 390, 391, 394(1), 395(1), 397(8), 404(22, 28), 407(1), 408(8), 409(1, 8, 60, 61), 412(60, 67, 71), 413(61), 415(61), 418(68, 85), 420( 1,68),422(1,68),427,429,430, 439 (20a, 20b), 451(38), 452(38), 456(5, 6), 458(57),467,462,464(2,3, 4),467(5, 7), 468(7, 10), 469(2, 7,11), 471(3, 7), 472 (7), 473(5, 7), 482(7, 27, 29), 483(3, 7), 484(7, 29), 487(3, 27, 29, 40), 488(29), 490(2, 27, 29, 45, 50), 491(29), 492(7), 493(7), 494(7), 495(50), 496(5), 497(50), 495, 499, 500, 527(110,112), 559, 558 (48), 580

Hill, J. A., 343(53), 349(53), 390 % Hinze, R. P., 219(58, 59), 242 Hirai, K., 239(102), 245 Hitchcock, P. B., 77(69), 105 Hitchman, M. A., 439(18), 440(23), 467 Ho, K. S., 117(26), 120(26), 137(68),

742, 744 Ho, R. K. Y., 308(63), 522 Hoard, J. L., 80(79), 105 Hodder, O. J. R., 33(39), 75(67), 103,104,

208(24), 224(24), 247, 345(60), 390 Hodgkin, D. C., 24(3, 4), 25(3), 26(11,

12, 13, 14, 15, 16, 17, 18, 19, 20), 27 (21), 28(22), 30(32), 33(34, 35, 36, 37, 38), 40(16), 47(22), 54(54), 69(59), 72(54), 75(67, 68), 78(76, 77, 78), 102, 103,104,105, 110(7), 747, 147(4), 764, 202(1, 3), 204(1, 10), 205(15, 16), 207(15, 20), 223(67), 224(67), 231 (88), 234(17), 240, 242, 243, 246 (1), 256, 296(1), 313(75), 579, 522, 342(43, 44, 45, 47, 48, 49), 344(47), 347(47), 559, 390, 407(59), 422(100), 429, 430, 432(5), 460, 467(9), 472 (9), 482(9), 495

Hodgson, G. L., 117(29), 118(29), 742

Hoffbrand, A. V., 161(70), 163(83), 766, 767

Hoffman, M. Z., 250(32), 257 Hoffman, P. J., 455(55), 462

Hussein, H. A. A., 161(70), 766

Iannarella, L., 338(35), 389 Ihara,M., 112(14), 113(14), 114(14b),

116(25), 117(25), 120(25b), 742, 218(56), 242, 482(25), 499

Ikeda, K., 116(23), 742, 338(33), 389

Imfield, M., 115(17), 126(55), 132(59), 742, 744, 318(93), 323

Ing, S. Y. S., 228(73), 242 Ingold, K. U., 567(58), 580 Ingraham, L. L., 248(12), 249(17), 256

(89), 257(89), 266(89), 284(17), 287, 289, 302(33), 314(77), 321, 322, 398 (11), 427, 534(155), 547, 556(45), 564(53), 575(86, 89), 580, 581, 582

Ingram, D. J. E., 461(14) Inhoffen, H.-H., 125(50), 744, 216(47),

219(58,59), 228(47), 247 Irion, E., 161(66), 766, 303(34), 312(71),

316(87), 527, 322, 323 Irvine, D. H., 412(66), 429 Irwin, A. J., 120(40), 123(40), 126(40),

127(52), 133(62), 134(62), 135(62), 137(62), 745, 744

Ishikawa, Y , 455(53), 456(53), 462

Itoh, N., 338(33), 389 Iwamoto, H., 150(19), 161(19), 764

Jackson, B., 163(83), 767 Jackson, W. R., 394(1), 395(1), 407(1),

409(1), 420(1), 422(1), 427 Jacobsen, D. W., 163(82), 767, 267(118),

297, 300(15, 16), 307(15), 320 Jaffe, H. H., 340(38), 389 Janata, E., 573(76), 557 Jaselskis,B., 418(87), 430 Jauernig, D., 239(101), 245 Jencks, W. P., 337(29), 352(63), 389,

390 Jensen, F. R., 254(75), 260(98), 268

(130, 131), 289, 290, 291, 317(88), 525, 512(57), 523(88), 525(57), 538

Jenson, L. H., 706(123), 117(26), 120 (26), 742

Joblin, K. N., 298(9), 299(13), 320, 553 (26), 576(91), 579, 582

Johansen, J. T., 468(13), 499

Hogenkamp, H. P. C 30(31), 54(53), 705, 104, 147(3), 164, 247(10), 251 (28), 255(79), 267(114), 268(124, 126, 127, 128, 129), 287, 289, 290, 291, 297(3, 4), 300(20), 301(24), 303(20, 27) , 304(24), 305(45, 47), 306(51, 55, 56, 57), 307(55), 310(55, 64), 312(47, 72), 313(55, 74, 76), 320, 321, 322, 331(11), 353(68), 354(69, 70), 388, 390, 391, 404(29), 405(46), 418(29, 31), 427, 428, 432(1, 3), 433(3), 439 (3), 440(22), 441(3), 442(3), 449(3, 33, 34), 455(55), 460, 461, 462, 478 (21), 482(24, 28), 486(36), 487(24, 28) , 488(21, 24), 489(21, 24), 490 (21), 492(46), 493(24, 28), 495(21, 51), 497(24, 51), 499, 500, 504( 14), 508(37), 524(37, 91), 525(37), 527 (114, 118, 119), 529(127), 536, 538, 539, 540, 545(3), 549(15), 552(20), 554(32), 578, 579

Holiday, E. R., 204(8), 215(8), 240 Holland, H. L., 282(192), 284(192), 293,

534(151), 541, 549(14), 575(84), 578, 581

Holland, R. J., 252(42, 43), 253(42, 43), 254(43), 255(43), 256(43), 267(118), 288, 291, 300(15), 307(15), 316(84), 320, 323, 363(82), 365(85), 391, 506 (24) , 507( 28), 524( 24), 527( 116), 536,539

Hollenstein, R., 115(18), 116(25), 117 (25) , 120(25b),742

Holloway,M. R., 576(91), 582 Holm, R. H., 438(16), 461 Holmes, A., 202 (5), 209( 5), 212( 5), 214

(5), 217(5), 227(5), 230(5), 240 Holmes, S., 247(10), 287 Holt, E. M., 706(118) Horig, J., 110(3), 120(3), 747 Horn, U. , 282( 192), 284( 192), 293, 534

(151), 547,575(84), 581 Horsley, W. J., 489(42), 500 Hoskins, B. F., 78(73), 105 Hosozawa, S., 118(34), 745 Howard, J., 539 Huennekens, F. M., 147(10), 157(57, 59), 158(57), 159(62, 63), 161(63), 162(75, 76, 77), 163(82), 764, 766, 167, 267(118), 297, 300(15, 16), 307 (15), 320 Huie, B. T., 280(180), 293 Hunt, E., 117(29), 118(29), 742

Johnson, A. W., 110(5, 7), 120(5), 747, 147(7), 156(45), 164,165, 202(2), 203 (37), 204(2, 11), 213(37), 215(2, 11), 216(43, 45), 218(2, 55), 220(2, 11, 55), 225(11), 226(11), 227(11), 230 (79), 231(11), 234(79, 80), 236(11), 238(11, 37, 99), 240, 241, 242, 243, 246(3), 252(3), 254(68, 69), 266(3), 267(112, 115), 271(147), 277(3), 281 (185, 186), 286, 289, 290, 292, 293, 297(6), 298(7, 9, 11), 302(29, 32), 305(46), 306(54), 318(54), 320, 321, 335(19), 340(37), 389, 417(81), 418 (89), 419(89), 429, 430, 508(34), 524 (34), 536, 538, 549(13), 553(26), 573 (78), 576(91), 578, 579, 581, 582

Johnson, E. A., 277(165), 292, 418(91), 430

Johnson, M. D., 226(93), 246(2), 256(2, 90), 257(93), 261(93), 263(93, 104), 265(93), 266(108), 267(108), 268(134), 269(136), 277(166), 285(204, 205), 286, 286(204, 205), 289, 290, 291, 294, 300(18), 320, 330(7), 335(7), 364(7), 365(7), 381(118), 388, 392, 504(8), 516(74), 517(8), 525(100, 101), 526 (100), 527(101), 536, 538, 539, 551 (18) , 568(63, 66), 569(63, 66, 67), 570 (63), 579, 580, 581

Johnson, R. A., 532(134), 534(134), 540 Jones, C, 144(11) Jones, H. E., 122(44), 143 Jones, I. D., 426(105), 430 Jones, J. R., 468(12), 499 Jones, K., 122(46), 123(46), 125(46), 126

(46), 128(46), 135(66), 143,144 Jones, W. H., 26(8), 102 Jonsen, J., 228(72), 242 Jordan, P. M., 118(34, 39), 143 J0rgensen, C. K , 409(64, 65), 429 Jorin, E., 441(25), 442(25, 26), 458(60),

459(60), 461, 462 Julita,P., 152(26), 154(26), 165

Kaczka, E., 239(104), 243 Kajiwara, M., 112(13), 115(19), 133(19), 137(68), 142,144, 218(52), 241, 473

(19) , 479(19), 480(19), 481(19), 499 Kallen, R. G., 248(14, 20, 21), 249(19),

287, 289, 308(62), 311(67), 322, 527 (117), 529(117), 539

Kamenar, B., 78(72, 73), 105 Kamin, H., 122(45), 125(45), 128(45), 143

Kammerer, P., 117(30), 143 Kamper, J., 26(14, 15), 102, 110(7), 141,

204(10), 2 05(16), 240, 407(59), 429 Kamper, M. J., 26(17, 19, 20), 27(21),

103, 342(43), 389 Kang, J., 377(98), 379(105,107), 392, 532

(143,144,145), 540, 565(56), 566(56), 580

Karrer, P., 204(9), 241 (49) Kasha, M., 402(20), 403(20), 406(58),

407(58), 427, 428 Kaska,W. C, 276(161), 292 Katada, M., 485(34), 499 Kato,T., 154(38), 165 Katz, J. J., 112(12), 142 Katz, R. N., 282(191), 293, 297(5), 307

(5), 316(86), 320, 323, 575(88), 581 Kaufman, E. J., 253(58, 59), 288 Kemball, C , 252(49), 288 Keese, R., 212(35, 36), 220(35, 36), 241,

345(61), 390 Keljo, D. J., 248(21), 287 Kemp, T. J., 284(198), 293, 303(39),

316(39), 321, 532(136, 137, 138), 534 (149), 540, 541, 553(24), 571(69, 73), 572(74), 575(73, I S ) , 579, 581

Kempe, U. M.. 269(139), 291, 377(101), 392, 533(146,147, 148), 540, 564 (54), 580

Kennedy, F. S., 297(120), 303(35), 311 (69), 312(69), 321, 322, 405(45), 428, 490(43), 500, 526(105), 527(110), 529 (105), 539

Kennedy, S. F., 303(36), 527 Kennedy, S. M., 267(115), 290, 298(11),

320, 573(78), 581 Kerr, J. A., 509(44), 531 (133), 537, 540 Kerwar, S. S., 156(51), 166, 548(11), 550

( 1 1 ) , 578 Khanna,P. L., 261(102), 290 Kharasch, M. S., 540(141) Kimball, M. E., 276(161), 292 King, N. K., 458(56), 462 King, T. J., 77(70), 105 Kishimoto, S., 121(41), 745 Kiskis, R. C., 268(131), 297, 512(57),

525(57), 537 Kistenmacher, T. J., 59(85), 85(85), 86

(85), 105 Kitchin, J. P., 317(91), 525 Klein, H., 137(68), 744 Klem, A., 249(26), 287 Klioze, S., 117(26), 120(26), 742

Laland, P., 249(26), 287 Laland,S., 228(72), 242 Lamm, F. P., 527(116), 539 Lappert, M. F., 267(115), 290, 298(9,

11), 320, 553(26), 573(78), 576(91) 579, 581,582

Larkin, J. P., 573(75), 581 Law, D. Y., 297(119) Law, P. Y., 298(10), 320, 469(15), 499 Lawson, W. B., 228(70), 242 Lee,E., 116(24), 117(26), 120(26), 742 Lee, h .,538

Kochi, J. K., 379(111, 115), 392, 556(41), 580

Kohlmiller, N. A., 495(51), 497(51), 500

Kohnle, J., 80(80), 105, 419(95), 430, 502(2), 535

Koketsu, N., 246(4), 254(62), 255(62), 256(62), 257(62), 263(62), 265(62), 286, 289

Kbnigk,E., 161(71), 166 Koniusky, F. R., 25(5), 102, 239(104),

243 Kopf, J., 92(127), 106 Lee, L. P., 277(168), 292, 308(63), 322

362(77), 365(77), 369(11), 391, 398 ' (14), 404(14), 406(14), 419(14), 427, 432(7), 439(7), 458(58), 460, 462, 508(36), 524(36), 536, 553(22), 579

Koppenhagen, V. B. , 37(41), 40(47, 48) ,72(60, 6 1), 74(41), 103,104, 211(27,28,29, 30), 241, 485(32), 499

Kosower, E. M., 409(63), 429 Krasna, A. J., 149(16), 164 Lee, S. L., 117(26), 120(26), 142 Krautler, B., 212(33), 241 LeGates, R., 248(18, 19), 249(18), 271

(18), 270(145), 276(145), 283(18), 287, 292

Krebs, T., 377(101), 392, 533(146, 147,148), 540, 564(54), 580

Kriemler, H.-P., 123(47, 48), 125(47, 48), 126(47), 127(47), 128(47), 129(59), 130(47), 132(48, 57), 133(62), 134 (48, 57, 62), 135(57, 60), 137(57, 62), 143,144

Legrand, M., 420(99), 430 Leigh, G. J., 549(10,578 Lenhert, P. G., 30(27, 28, 30), 41(30),

54(28), 59(28), 61(28), 64(28), 80 (81), 85(88), 87(88), 88(88), 103,105, 110(7), 747, 147(4), 764, 207(18), 208 (18), 240, 246(1), 286, 341(42), 342 (42), 344(42), 354(42), 355(42), 359 (42), 389, 391(14), 398(12), 427, 432 (6), 442(6), 460, 467(8), 472(8), 490 (8), 498, 505(21), 506(21), 514(21), 536, 550(16), 551(16), 579

Krodel, E. K., 65(56), 104, 282 (188), 283(188), 284(188), 293, 579(11)

Krouwer, J. S , 576(92), 578(U, Id), 582

Krueger, G. J., 706(105) Krusic, P. J., 379(115), 392 Kuehl, F. A., 218(53, 54), 241, 242 Kuhlmann, K. F., 477(20), 492(20), 499 Kuhn, H., 396(2), 398(2), 400(18), 401

Lenoir, D., 255(76), 261(76), 289 Lenp, J., 404(44), 428 Leont'eva, Ye. V., 379(113), 392

(2, 18), 402(21), 403(21), 420(21), Leopold, J. G., 318(95), 323 427 Lerner, D., 404(42), 418(42), 419(42), 428

Kurganov, B. I ., 305(49, 50) , 306(49, 50), 321

Levitin, I. Y., 516(72, 73), 538 Lewis, J., 539

Kustanovich, I. M., 284(202), 285(202), Lewis, N. G., 133(61), 134(61), 135(61), 293, 575(85), 581

Kwiatek, J., 292(163), 538 Kyaw, M., 218(97), 319(97), 323, 376

137(61), 744 Lexa, D., 252(46), 253(46), 288, 318(92),

323, 337(26), 364(84), 389, 391, 506 (92), 391 (25), 514(25), 522(25), 536

Li, T. K., 423(102), 430 Licare,T., 537 Laas, H., 2 16(47), 219(59), 228(47),

241, 242 Liebman, M., 47(50, 51, 52), 104 Lien, E. L., 297(119), 469(15), 499 Lindsey, J., 26(11, 15, 18), 102, 103,106, 205(16), 240, 342(44), 389, 407(59), 422(100), 429, 430, 467(9), 472(9), 482(9), 498

Ladd, J. N., 30(31), 54(53), 103,104, 296(2), 297(3), 312(73), 319, 320, 321, 353(68), 390

Ladd,T. M., 156(47), 765 Lake, R. E., 85(90), 105

Lindstrand, K., 147(6), 161(67), 164, 166

MacKay, M., 110(7), 141, 407(59), 429 McKenna, W.,547

Linhard, M., 428(49) McKenzic, E. D., 279(175, 176, 177), 282(177), 285(204), 286(204, 206), 292, 293, 294, 336(25), 381 McKervey, M. A., 576(93), 582 McLaughlin, G. M., 77(69), 105 McPhail, A. T., 106(116), 249(25), 254

Linnell, J. C, 161(68, 69, 70), 163(83), 166, 167

Lipscomb, J. D., 539 Livant, P., 549(12), 578 Ljungdahl, L., 161(66), 166, 303(34),

(24), 278(25), 287 MacQuitty, J. J., 267(115), 298(11), 290,

321 Lloyd, D., 212(34), 241

320, 573(78), 581 Madan, V., 260(98), 268(130), 290, 291,

Lockman, B. L., 285(205), 286(205), 294, 525(100, 101), 526(100), 527

317(88), 323, 523(88), 538 Magnuson, R. H., 516(73), 538 Mahcr, J. P., 273(152, 153), 292, 502(1), 511(47), 518(47), 526(1), 529(1), 535 (1,47), 535, 537 Mahoncy, M. J., 156(53), 166 Maillard, P., 404(39), 405(39), 418(39),

(101), 539 Locwenstein, A., 490(45), 500 Lohaus,G., 213(38), 241 Long, K. M., 250(33), 287, 404(35), 406

(54), 418(35), 428 Longworth, J. W., 426(107), 430 Looney, F. D., 432(2, 3), 433(2, 3), 439

419(39), 428, 553(23),579 Majerus, P. W., 268(121), 291 Maki, A. H., 438(16), 461 Mamalis, P., 352(64), 365(64), 390 Mann, B. E., 343(52), 345(59), 346(52), 347(52), 348(52), 349(52), 350(52), 351(52, 59), 353(59, 66), 354(52), 362(52), 369(52), 390, 397(8), 408 (8), 409(8), 418(85), 427, 429, 464 (3), 469(3), 471(3), 482(29), 484(3, 29), 487(3, 29), 488(29), 490(2, 29), 491(29), 494(3), 498, 499 March, J., 337(28), 389 Margum, J. H., 163(78), 166 Marshall, D. R., 212(34), 247 Marsich,N., 317(90), 323 Martella, J. P., 276(161), 292 Martin, A. H , 272(150), 277(150), 292 Martin, H., 396(2), 398(2), 401(2), 427 Martin, J. C, 549(12), 578 Marwaha, L. K., 377(99), 379(99),

(3, 21), 441(3), 442(3, 21), 443(21), 444(21), 445(21), 449(3, 21), 458(56), 460, 461, 462

Loots, M., 512(52), 537 Lovenberg, W., 163(84), 167, 254(71),

289 Lovtsova, A. N., 379(113), 392 Lowc,D. J.,299(13), J20 Lu, L.-Y., 278(173), 292 Lu, S. H., 110(3), 120(3), 141 Luthy,J., 115(22), 142 Lyles, D., 248( 14), 249( 14), 28 7, 308

(62), 322 Lynen,F., 532(139, 140), 540

Maag, H., 202(5), 209(5), 212(5), 213 (40), 214(5), 217(5), 227(5), 230(5), 240, 241

McAuliffe, C. A., 388(3) McAuslan, B., 156(51), 166 Maccoll, A., 338(30), 389

392, 567(62), 580 Marx, J. N., 258(96), 290 Marzilli, L. G., 85(83, 85, 87), 86(83, 85, 95), 88(83), 105, 273(156), 275(156), 292, 359 (72), 375(72), 382(72), J97, 491(47), 500, 505(18, 20), 506 (20), 518(80), 519(81), 531(18, 20), 535(80, S I ) , 536, 538 Marzilli, P. A., 273(156), 275(156), 292,

McDonald, E., 111(8), 112(11, 14), 113 (14), 114(146), 115(18), 116(8, 25), 117(25, 28, 29, 31, 32, 33, 35, 36, 37), 118(28, 29, 33), 120(25b), 121(41), 122(43, 46), 123(40, 43, 46), 125(43, 46, 51), 126(46, 51, 53), 127(28a), 128(46), 129(43, 56), 130(56), 132 (49, 60), 133(60, 61), 134(61), 135 (43, 60, 61), 137(61), 142, 143, 218 (56), 242, 482(25), 499

518(80), 519(81), 535(80, 81), 538 Mason, H. S., 432(1), 460 Masuda, I., 406(55), 419(55), 428

McFadden, D. L., 106(116) Mackay, M ., 26( 14, 15) , 102, 204(10),

205(16), 240

Matcham, G. W. J., 117(28, 32, 33), 118 (28,35,36,37), 127(28a), 132(60), 133(60, 61), 134(61), 135(60, 61), 137

Mildvan, A. S., 65(56), 68(57), 104, 382 (121), 392, 451(37), 462, 558(47) 559(47), 579(11), 580

Miller, I. M., 116(23), 142 Miller, I. W., 111(9), 142 Milton, P. A., 494(49), 496(49), 500 Mingardi, M., 406(56), 428 Minghetti, A., 152(26), 154(26), 165 Mitchell, T. R. B., 576(93), 582 Mok, C. Y., 503(5), 508(5), 524(5), 525

(61) , 142, 143,144 Math, V. B., 33(39), 103, 208(24), 222

(65), 223(65), 224(24), 234(65), 236 (65), 241, 242, 345(60), 390, 485(33), 499

Mathews, D. M., 161(68, 69, 70), 166 Matsuda, A., 300(17), 320 Matsumoto, H., 118(34), 143 Matsumoto, J., 150(19), 161(19), 164

( 5 ) , 535, 554(28), 579 Molander, G. A., 260(100), 290, 539 Mombelli, L., 144(10) Monkjaro, Y., 300(15), 307(15), 320 Montejano, Y., 267(118), 291 Montforts, S., 135(66), 144 Montgomery, L. K., 567(59), 580 Moore, F. H., 33(35, 36), 103, 205(15),

Matt, J. W., 567(59), 580 Mattern,C. F. T., 30(29), 103 Matwiyoff, N. A., 268(127, 128, 129),

291, 301(24), 304(24), 313(76), 320, 322, 354(70), 391, 404(31), 418(31), 428, 478(21), 479(22), 482(24), 484 (22), 487(22, 24), 488(21, 24), 489 (21, 24), 490(21), 492(46), 493(24, 48), 495(21,51), 497(24, 51), 499, 500, 552(20),579

207(15), 240, 342(47), 344(47), 347 (47), 390

Moore, F. M., 231(88), 243, 313(75), 322

Moore, K. W., 554(30), 555(30), 579 Moore, M., 218(54), 242 Morallee, K. G., 490(45), 500 Morley, G. G. D., 313(74), 322, 574(80), 581

Mauck,L., 555(34), 579 Mayer, E., 344(55), 390, 398(10), 427 Mays, M. J., 276(162), 292 Meegan, M. J., 117(32, 33), 118(33),

143 Morris, H., 122(43, 46), 123(43, 46), 125 (43,46), 126(46), 128(46), 129(43), 135(43), 143

Meeks, B. S., 256(93), 257(93), 261(93), 263(93, 104), 265(93), 290

Merienne, C, 256(74), 264(74), 289, 304(42), 321, 364(83), 391, 404(37), 405(37), 418(37), 428, 511(49), 512 (55), 525(55), 537

Morris, H. R., 132(60), 133(60), 135(60), 144

Moskophidis, M., 267(116), 290, 301(27), 320

Merle, G., 525(95), 539 Moss,T. H., 381(120), 392, 449(28, 32), 450(32), 451(28, 32), 453(32), 461, 558 Mervyn, L. , 147( 7), 156( 45), 164, 165,

224(68), 242, 254(68, 69) , 2 67(112),271(147), 289, 290, 292, 429

(49), 580 Mueller, O., 268(123), 291 Muggleton, P. W., 271(147), 292 Miiller, G., 117(27, 30), 123(47, 48), 125 (47,48), 126(47), 127(47), 128(47), 129(57), 130(47), 132(48, 57, 59), 133 (62), 134(48, 57, 62), 135(57, 62), 137

Messerschmidt, R. , 413( 72, 73, 7 4, 75, 76), 415(72), 429

Mestroni, C., 254(63, 65), 256(91), 270 (91), 271(146), 277(170, 171), 280 (91), 289, 290, 292, 301(28), 320, 336 (24), 389, 502(3), 514(3), 525(99), 526(109), 535, 537,539

(57, 62), 143,144(10), 150(18), 164, 235(90), 236(90), 243 Mullcr, N.,500 Meyer, E. F., 241(25),

Meyer, E. F., Jr., 75(62, 63), 78(62), 80 Miiller, O., 148(14), 150(18), 164, 235 (90), 236(90), 243, 254(67), 289, 429 MUller, R. M., 212(33), 241 MUller, U. G., 429 Munch, E.,539

(62) , 104 Meyerstein, D., 574(81), 581 Michaely, W. J., 316(84, 85), 323 Michna, H , 110(2), 120(2), 141, 231

Munch-Peterson, A., 156(47), 165 Murakami, M., 150(19), 161(19), 164

W ) , 243 Migliacci, A., 152(26), 154(26), 165

Murie,R., 239(103), 243 Obata, N., 202(5), 209(5), 212(5), 214 (5), 217(5), 227(5), 230(5), 240 Murphy, M. J., 122(45), 125(45), 128

(45), 143 Murphy, S., 157(57), 158(57), 166 Myers, C, 156(52), 160(52), 166 Myerstein, D., 292(151)

Ochiai, E ., 250( 33), 287, 404(35), 406(54), 418( 35), 428, 450(42), 462

Ochiai, E.-L, 556(37), 578(94), 579, 582

Nardelli,M., 106(110) O'Connor, B. H., 33(36), 103, 205(15), Nardin, G., 343(51), 349(51), 360(51), 207(15), 240, 342(47), 344(47), 347

390, 505(16), 531(16), 536 Nath, A., 485(34), 499 Naumberg, M., 253(53), 256(53), 257

(47), 390 Oester,M. Y., 125(50), 144 Offenhartz, B. H., 396(3), 397(9),

(53), 263(53), 265(53), 288, 524(90), 401(3), 427 Offenhartz, P. O., 397(9), 427 Ofner, S., 135(66), 144 Ogawa,H., 317(89), 323 Ogoshi, H., 246(4), 254(62), 255(62),

538 Needham, T. E., 268(127, 128, 129), 291,

478(21), 488(21), 489(21), 490(21), 493(48), 495(21), 499, 500

Neier, R., 129(56), 130(56), 144, 239 256(62), 257(62), 263(62), 265(62), (102), 243

Neler, R., 132(60), 133(60, 61), 134 286, 289

Ohashi, Y., 88(96, 101, 102, 103), 89 (61), 135(60, 61), 137(61), 144

Nelson, J. H., 106(11%) Nemeth,S., 253(60, 61), 288 Neri,C., 280(182), 293 Nerone, A., 85(92), 105 Neta, P , 571(68, 71,72), 581 Netzel, T. L., 299(14), 320, 363(79),

(104,115), 90(101), 105,106 Ohgo, Y., 88(102, 103), 89(115), 106 Ohta,H., 160(65), 166 Oikawa, T. G., 305(47), 312(47), 321 Okada,K., 113(13), 142, 218(52), 241,

473(19), 479(19), 480(19), 481(19), 499 Oldfield, D., 297(6), 320 Oleson, H., 414(78), 417(78), 423(78), 376(79), 391, 404(40), 405(40), 418

(40), 428 Neumann, E., 137(68), 144 Newman, M. S., 231(86), 243 Nex0, E., 268(122), 291, 414(78), 417

429 Olivella, S., 567(60), 580 Olson, C. D., 440(23), 461 Oltersdorf, U., 225(69), 228(69), 242 Orgel, L. E., 338(30, 31), 389 Orme-Johnson, W. H., 381(120), 392,

(78), 423(78), 429 Ng, F. T. T., 508(42), 510(42, 45), 511

(42), 530(42), 535(42), 537 Nicholson, B. K , 298(9), 320, 553(26),

441(32), 450(32, 35), 451(32), 453 (32), 455(35, 52, 53), 456(52, 53),

579 461,462, 558(49, 50), 580 Ostroy,F., 156(54), 166 Overath, P., 532(139, 140), 540 Overend, W. R., 203(37), 221(37), 213

Nocchi, E., 303(39), 316(39), 321, 508 (39), 525(39), 534(149), 537,541, 553 (24), 571(69, 73), 575(73), 579, 581

Nockolds, C. E., 33(36), 103, 33(34, 36), 103, 205(15), 207(15), 240, 342(47), 344(47), 347(47), 390

(37), 238(37, 99), 241, 243

Page, J. E., 25(7), 102 Nome, F., 304(43), 321, 409(62),

429 Pailes, W. H., 251(28), 287, 303(37), 321,

597(71), 405(46), 428, 524(91),538 Nordlov,H., 118(34), 143 Palmieri,C. G., 706(110) Nordmeyer, J. P., 249(27), 287, 301(26), Pannhorst, W., 87(97, 99), 88(97, 99),

105, 269(139), 270(141,142), 297, 379(104, 106), 392, 533(146, 147, 148), 540, 565(57), 580

320, 413(72, 73, 74, 75, 76), 415(72), 429

Norman, R. O. C, 532(135), 534(135), Parfenov, E. A., 282(189, 190), 284(199,

200, 201, 202, 203), 285(200, 202), 293, 294, 549(14), 575(85), 578, 581

540, 573(75), 581 Nussbaumer, C., 144(10) Nyholm, R. S., 330(38), 389

Pilbrow, J. R., 381(119), 382(119), 392 432(8), 433(9), 434(9), 437(9,10), ' 438(12a, 12b), 439(8, 9, 19, 21), 440 (9, 24), 442(21), 443(21), 444(21), 445(21), 449(21), 452(50, 51), 453 (9, 44, 50, 51), 454(44), 457(9, 44), 460, 461, 462(59), 559(51), 580

Park Y., 275(159), 292, 335(21), 389 Parker, I. H., 438(17), 439(17), 467 Parker, L. F. J., 12(2), 13(2), 15, 25(7),

102, 110(5), 120(5), 141, 204(11), 215(11), 220(11), 225(11), 226(11), 227(11), 230(79), 231(11), 234(79), 236(11), 238(11), 240, 418(80), 429

Parry, R., 469(14), 499 Patchornik, A., 228(70), 242 Pawelkiewicz, J., 154(38), 165, 230(81),

Pilling, D., 26(19), 103, 342(43), 389

Pinnock, H. A. , 245( 100), 246 (3), 252(3), 266(3), 277(3), 286, 302(32), 527

242, 267(113), 290 Payne, M. D., 85(91), 105 Pearson, R. G., 250(36), 288 Pellizen, A., 502(3), 514(3), 555 Pellizer, G., 254(65), 256(91), 270(91),

Poe, M., 343(58), 344(58), 349 (58), 350(58), 354(58), 390, 469(16), 471(17), 486(17), 487(17), 499 280(91), 289, 290, 301(28), 320, 336

Porter, G. B., 406(56), 428 (24), 389, 490(45), 500 Pencovici, M., 248(14), 249(14), 287, Porter, M. W., 24(3), 25(3), 102

Pospelova, T. A., 267(111), 290, 305 (49, 50), 306(49, 50), 527

308(62), 322 Penley, M. W., 307(59), 322, 490(50),

Postgate, J. R., 122(44), 745 495(50), 497(50), 500 Peng, S., 335(21), 389 Peng, S.M., 275(159), 292 Perego,G., 280(182), 293 Perlman,D., 306(52), 321 Perree-Fauret, M., 251(39), 279(179), 288,

Poston, J. M., 147(8), 155(8), 764, 528 (121), 559

Poznanskaya, A. A., 267(111), 290 Pratt, J. M., 158(60), 766, 228(71), 242,

255(77, 81, 82, 83), 289, 300(19, 21), 303(21), 311(69), 312(69), 314(78), 320, 322, 329(1, 2, 4), 330(2, 6), 333 (1,2, 12), 335(2, 4, 6, 14,16), 336 (2, 27), 337(2), 342(2), 343(2, 52, 53, 54), 344(2, 54), 345(2, 59), 346(52), 347(2, 52), 348(52), 349(2, 6, 52, 53), 350(2, 52), 351(2, 52, 54, 59), 352(54), 353(2, 54, 66), 354(2, 52), 355(2, 54), 357(54), 358(54), 359(2, 54), 360(54), 361(4, 6, 75), 362(52, 54, 78), 363(2), 364(2, 54), 365(54, 86), 366(2, 54), 367 (6), 368(54), 369(52), 371(54), 373(90), 374(2), 376(54), 377(4), 379(78), 380 (86), 381(4), 385(4), 386(4), 388, 389, 390, 391, 394(1), 395(1), 404(22, 27, 28, 33, 34), 405(34), 407(1), 409(1, 60), 412(27, 60, 67, 69, 71), 413(61), 415 (61), 418(33, 34, 68, 85), 419(69, 97), 420(1, 68), 422(1, 68), 427, 428, 429, 430, 439(20a, 20b), 464(2, 3, 4), 468 (10, 11), 469(2, 11), 471(3), 482(26, 29), 484(3, 26, 29), 485(26), 487(3, 26, 39), 488(29), 490(2, 26, 29, 50), 491(29), 492(26), 494(3), 495(50), 497(50), 498, 499, 500, 504(6, 9), 508(9, 35), 524(35), 527(110), 535, 556, 539, 567(61), 580

293 Perrin, D. D., 277(172), 292 Perrin,D. R., 277(172), 292 Perrotti, E., 280(182), 293 Pesaro, M., 236(96), 247(39), 243 Peterkofsky, A., 156(44, 49, 50), 159

(49), 160(64), 163(50), 165,166 Petersen, R. L., 485(34), 499 Petrocine, D., 115(19), 133(19), 742 Petrova, R. G., 556(42), 580 Petrow, V., 26(9), 102, 204(8), 215(8),

240, 352(64), 365(64), 390 Pezacka, E., 154(39), 765 Pfaltz, A., 212(33), 221(61), 239(102),

247, 242, 243 Pfenninger, A., 744(71) Pfiffner, J. J., 72(60, 61), 104, 211(27,

28, 29, 30), 228(73), 247, 242 Phelan, P. F., 273(154, 157), 275(157),

292, 518(22), 519(22), 535(22), 536 Phillips, C. S. G., 338(32), 339(32), 389 Phillips, G. O., 318(94, 96, 97), 319(97),

323, 376(91, 92), 391 Pickworth, J., 26(11), 702, 26(11, 12,15,

16), 40(16), 102,103, 110(7), 747, 202(1), 204(1, 10), 205(16), 234(17),

Pribanic,M., 335(16), 389 240, 342(48, 49), 390, 407(59), 429

Prince, R. H., 266(106), 290, 539 Pritchard, D. E., 500(44) Pritchett, J., 532(135), 534(135), 540 Prosen, R. J., 26(12, 15, 16), 40(16), 103,

Renz, P., 110(3), 120(3), 141, 152(22, 23), 153(22, 35), 154(35), 165, 216 (44), 226(44), 241

Retey, J., 87(98, 99, 125), 88(98, 99), 105,106, 115(22), 142, 261(101), 269 (137,139), 270(141, 142), 290, 291, 377(96, 101, 102), 378(102), 379(104, 106), 381(102), 384(102), 385(102), 391, 392, 533(146, 147, 148),540, 545(4), 558(4, 46), 564(54), 565(57), 577(4), 578, 580

202(1), 204(1), 205(16), 234(17), 240 Prout,C. K., 78(72, 73), 105 Pryde, L. M., 118(34), 143 Pullman, B., 396(4), 398(4), 427 Puxeddu, A., 250(35), 256(91), 270(91,

143), 271(143), 280(91), 290, 336(24), 389, 514(61, 62), 537

Puxeddu, E., 502(3), 514(3), 535 Reutov,0. A., 379(112), 392 Reynhardt, E. C., 706(105)

Quadros, E. V., 161(68, 69), 163(83), Rhee,S. G., 352(65), 390 166,167

Que, L , 559(104) Quillivia, R., 300(18), 320

Ribiero, A., 308(63), 322 Ricchiero, F., 404(42), 418(42), 419(42),

428 Richards, J. C., 404(43), 428 Richards, J. H., 449(31), 467, 554(30), Radmer, R., 118(38), 143

Radom,L., 452( 47), 462, 532(136, 137,138), 540, 556(36), 557( 36), 558( 36),559(36), 573(36), 579

555(30), 571(69), 579, 581 Richardson, K., 243(100) Rickes,E. L., 25(5), 102, 239(104), 243 Ridley, W. P., 539 Rahn,R. O., 426(107), 430

Raleigh, J. A., 231(87), 233(87), 243 Ridsdale, S., 255(82), 289, 490(50), 495 Ramaseshan, S., 33(34), 103 (50), 497(50), 500

Ridsdale, S. C., 311(69), 312(69), 322, Randaccio, L., 85(82), 86(82, 95, 111), 87(112), 88(82), 105, 106(106, 107, 108, 109), 343(51), 349(51), 359 (72), 360(72), 375(72), 382(72),

527(110), 539 Rietz, P., 231(84), 243 Ritari, S. J., 163(80), 767 Robertson, J. H., 26(11, 12, 15, 16), 28 390, 391, 505(16, 17, 18, 19, 20),

506(20), 531(16, 17, 18, 19, 20), 531 (20), 536

(24), 102, 103, 202(1), 204(1), 205 (16), 234(17), 240, 407(59), 429

Robinson, J. A., 122(46), 123(46), 125 Randacew, L., 491(47), 500 Rapp, P., 110(2), 120(2), 141 (46), 126(46, 53), 128(46), 143,144, Rapp, R., 110(2), 120(2), 141, 225(69), 270(140), 297

Roche, J. S., 271(149), 272(149), 292 Roche, T. S., 246(6), 271(6), 287, 335

228(69), 231(89), 239(101), 242, 243 Rasetti, V., 135(66), 144 Redfern, J. R., 218(56), 242, 482(25), (13), 389, 515(70), 516(70), 535(70),

499 538 Redfield, B. G., 156(44, 50), 163(50),

165,166 Rodrigo, R. , 21 6(45), 247, 29 7(6), 302

(29), 306( 54), 318( 54), 320, 321 , 418 (89), 419( 89), 429, 430, 508(34), 524 (34), 536

Redmond, J. W., 115(21), 142, 204(12), 212(12), 221(62), 231(87), 233(87), 235(62), 236(93), 240, 243 Roewer,G., 553(27), 579

Reenstra, W. W., 352(63), 390 Ronzio, R. A., 152(27), 765 Reetz, M. T., 556(40), 580 Rooney, J. J., 576(93), 582 Rehorek,D., 553(27), 579 Rosales, F., 163(80), 767 Reisenhofer, E., 250(35), 256(91), 270

(91,143), 271(143), 280(91), 288, 290, 291, 336(24), 389, 502(3), 514(3, 61, 62), 535, 537

Rose, I. A., 562(52), 580 Rosen, C. G., 526(105), 529(105), 539 Rosenberg, L . E., 156( 53, 55) , 157( 56),

766 Rempel, G. L., 508(42), 510(42, 45),

511(42), 530(42), 535(42), 537 Rosenblum,C., 1 11(9), 742, 14 9(16),

764

Schevlin,P. B., 556( 43), 580 Schiebel, H. M., 219(59), 242 Schilling, W., 202(5), 209(5), 212(5),

Rosenthal, D., 122(45), 125(45), 128 (45), 143

Rowe, J. N., 564(53), 580 Rubin, E. M., 363(82), 391 Rubison, K. A., 241(31), 426(104), 430 RUchardt,C, 548(10), 578 Rudakova, I. P., 255(78), 267(109, 110,

214(5), 217(5), 227(5), 230(5), 240

Schindler, O., 419(93), 430 Schlecht, M., 268(123), 291 Schlingman, G., 485(32), 499 Schlingmann, G., 40(48), 104 Schmid, H., 204(9), 240, 241(49) Schneider, P., 202(5), 209(5), 212(5), 214(5), 217(5), 227(5), 230(5), 240 Schneider, P. W., 273(154), 292 Schneider, Z., 154(40), 155(40), 165 Schonland, D. S., 461(14), 461 Schrauzer, G. N., 80(80), 105, 109(1), 141, 158(61), 166, 240(21), 246(7), 247(8, 9), 248(13), 250(30, 31), 251 (13), 252(9, 42, 43), 253(30, 42, 43, 56), 254(31, 43, 70), 255(43), 256 (8, 43, 88), 257(94, 95), 258(31, 97), 262(103), 263(103), 269(8), 277(13, 168, 169), 278(13), 282(191), 283(88), 287, 288, 289, 290, 292, 293, 297(5), 300(22), 301(22), 302(22, 31), 303 (22), 304(40, 41), 305(48), 307(5, 48, 58), 308(63), 311(48, 58, 66, 68), 312 (48), 313(31, 58), 314(31), 316(84, 85, 86), 320, 321, 322, 323, 351(62), 352 (62), 357(62), 358(62), 362(62, 77), 363(82), 364(62), 365(77, 85), 366(87, 88), 367(62), 368(62), 369(62, 77), 370 (62), 371(62), 373(88), 376(88), 390, 391, 397(5), 398(13, 14), 404(13, 14, 30), 406(14), 418(30), 419(14, 30, 95, 96), 427, 430, 432(7), 439(7), 458(58), 460, 462, 502(2), 506(24), 507(28, 33), 508(36), 511(50), 518(78), 523(87), 524(24, 33, 36), 525(33), 527(115, 116), 529(115), 530(129, 130), 535, 536, 537, 538, 539, 540, 547(7), 549(7), 551 (19), 552(21), 553(21, 22), 559(7), 571(70), 575(88), 577(7), 578, 579, 581

117), 285(117), 289, 290, 298(8, 12), 299(12), 305(49, 50), 306(49, 50), 320, 321, 363(80, 81), 391, 513(58), 537, 573(77), 581

Ruoff,G., 239(101), 243 Rush, J. E.,289(S6),289, 306(55), 307

(55), 310(55), 313(55), 322, 527(114), 539, 549(15),579

Russell, G., 554(31), 579 Russell, G. A., 404(23), 427 Ryel, E. M., 156(54), 166

Sadler, P. J., 487(40), 500 Saito,T., 276(164), 292 Sakami, W., 163(80), 167 Sakrikar, S., 282(192, 193), 284(192),

293, 534(151, 153),541, 575(84), 581

Salama,S., 343(57), 390 Salem, L., 398(15), 400(15), 411(15),

419(15), 427, 530(131), 540, 556(38), 562(38), 564(38), 576(38), 579

Sander, E. G., 337(29), 389 Sando, G. N., 306(56), 322, 331(11),

388, 455(55), 462, 529(127), 540, 545 (3), 578

Sands, R. H., 382(122), 392, 450(41), 451(141), 453(41), 454(41), 462, 558 (47), 559(47), 580

Sasada, Y., 88(101, 102, 103), 89(104, 115), 90(101), 105, 106

Sato, K., 461(29), 545(5), 578 Satoh, F., 116(25), 117(25), 120(25b),

121(41), 142, 143 Saunders, J., 117(29), 118(29), 142 Saveant, J.-M., 252(46), 253(46), 318

(92),323, 337(26), 364(84), 389, 391, 506(25), 514(25), 522(25), 536

Schaefer, W. P., 280(180), 293 Schaeffer, E.,280(183, 184), 281(183,

Schreiber, J., 202(5), 209(5), 212(5), 213(40), 214(5), 217(5), 227(5), 230 (5), 240, 241

184), 293 Schaffler, J., 261(101), 290 Schaffner, T. J., 240(19) Scheffold, R., 236(96), 243 Schepler, K. L., 382(122), 392, 450(41),

Schreiner, A. F., 426(105), 430 Schulten, H. R., 219(59), 242 Schwartz, S., 116(23), 142 Schweiger, A., 441(25), 442(25, 26),

458(60), 459(60), 461, 462 451(41), 453(41), 454(41), 462 Scopes, P. M., 222(66), 242

Scott, A. I., 112(13), 113(16), 115(19), 116(24), 117(26), 118(34), 120(26,40), 123(40), 126(40), 127(52), 133(19, 62), 134(62), 135(62), 137(62, 68), 742,143, 144, 218(52), 241, 379(105, 107), 392, 393, 473(19), 479(19), 480(19), 481(19), 486(37), 499, 500, 552(144, 145), 540, 565(56), 566(56), 580

Shimizu, S. , 253( 57), 288, 301(25), 302 (30), 311( 65), 320, 321, 322, 508(38), 522(84), 524(38), 525(38), 536, 538

Shmyrev, I. K., 284(199), 295,549(14), 578

Shoemaker, C. B., 26( 15), 103,205(16), 240

Shoolery, J. M., 127(52), 144 Shoolery, J. N., 120(40), 123(40), 126 Seek, J. A., 363(82), 391

Seehra,J.S., 118(39), 143 (40), 745 Shulman, R. G., 426(107), 430 Shunk,C.H., 218(53), 247 Shveima, J. S., 525(97, 98), 559 Sibert, J. W., 247(9), 251(9), 252(9), 254 (70), 287, 288(31), 289, 300(22), 301 (22), 302(22), 303(22), 305(48), 307 (48), 311(48, 68), 312(48), 320, 321, 322, 362(77), 365(77), 366(87), 369 (77), 597, 398(14), 404(14, 30), 406 (14), 418(30), 419(14, 30), 427, 507 (33), 508(36), 524(33, 36), 525(33), 530(129), 536, 540, 553(22), 579 Siebert, H., 425(47)

Segal, G., 398(15), 400(15), 411(15), 419 (15), 427, 530(131), 540, 556(38), 562 (38) , 564(38), 576(38), 579

Segnitz, A., 295(178) Seible, J., 377(96), 391, 545(4), 558(4),

577(4), 578 Seki,H., 318(93), 525 Sell, C. S., 284(198), 295, 452(48), 462,

532(136, 137, 138), 534(136), 540, 572(74), 575(75), 581

Sellars, P. J., 268(125), 284(198), 291, 293, 381(116), 592, 452(48), 462, 553 (24), 568(64, 65, 66), 569(64, 65, 66), 570(65), 571(69), 572(74), 575(75), Siegel, L. M., 120( 40), 122( 45), 123( 40),

125 (45), 126(40), 127 ( 5 2), 128(45) ,745, 744

579, 580, 581 Sellers, P. J., 303(39), 316(39), 321, 508

Sigan, A. L.,55#(68a, b) (39) , 525(39, 97, 98), 532(136, 137, 138), 534(136), 557, 559, 540 Silverman, R. B., 248(15, 16), 281(15, 16,

187), 282(15, 16,187,188,194), 283 (187, 188,195,196, 197), 284(188, 197), 287, 293, 315(79, 80, 81, 82, 83), 316(82, 83), 522, 525, 534(152, 154, 156), 547, 575(83, 87), 557

Septe, B., 404(36), 405(36), 406(36), 418(36), 419(36), 428

Seyler, J. K., 292(163) Shapiro, M., 377(98, 99, 103), 379(99),

592, 532(142, 143), 540, 564(55), 565 (55), 566(55), 567(62), 580

Shatkina,T. N., 379(112, 113), 592 Shaw, N., 147(7), 156(45), 164, 165,

Simandi, L. I ., 248( 23), 252( 23, 47, 50, 51), 253(47, 60, 61), 287, 288

Sinke,G. C., 509(43), 557 Sinn, E., 92(128), 106 216(43), 241, 254(68, 69), 267(112), Skinner, H. A., 508(40), 557 271(147), 289, 297(6), 290, 292, Skyring,G.W., 122(44), 745 298(7), 305(46), 320, 321, 429

Sheldrick,G.M., 70(5(117), 266(106,107), Smith, C., 270(145), 276(145), 292 Smith, E. L., 25(6, 7), 102, 110(5), 120

(5), 747, 147(5, 7), 153(29), 156(45), 163(81), 764, 765, 767, 202(2), 204 (2, 11), 215(2,11), 218(2), 220(2,11), 225(11), 226(11), 227(11), 230(79), 231(11), 234(79), 236(11), 238(11), 240, 254(68, 69), 267(112), 271(147), 289, 290, 292, 418(80), 429

290 Sheldrick, W. S., 37(41, 42, 43, 44), 39(43),

40(42, 47), 74(41, 42), 103,104, 229 (74), 230(78), 242

Shelton, G , 77(70), 105, 281(185), 295, 340(37), 389

Shemin,D., 111(9, 10), 112(12), 218(51), 142, 241

Shepler, K. W., 558(47), 559(47), Smith, L. E., 12(2, 3), 13(2), 75 Smith, S. G., 490( 50), 49 5(50), 497( 50),

500 580

Shermin, D., 486(39), 500 Smith, T. A., 156( 52), 160( 52), 7 66, 548

(11), 550(11), 578 Shida, T., 318(93), 525 Shima, K., 406(55), 419(55), 428

Stotter.N. E., 106(111) Stout, G.H., 106(123) Stull, D. R., 509(43), 557 Sturgeon, B., 352(64), 365(64), 390 Subbarow, Y., 3(1), 4(1), 15 Subramanian, S., 338(34), 389 Suckling, C. J , 558(46), 580 Sundaralingam, M., 65(55), 104 Sutherland, I. O., 202(2), 204(2), 215

Smith, T. D. , 3 81(119), 382( 119), 592,438(12a, 12 b), 452( 44), 45 3(44, 50,51), 454(44), 457(44), 467, 462(59)

Smith, T. D.S., 559(51), 550 Smucker, L., 52/(38), 404(32), 405(32),

418(32), 428, 524(92), 538 Smyth, R. D. , 147( 1, 2) , 15 6(47), 164,

165, 296(2), 312 (73), 319, 322, 331 (9), 367(9), 388

Sneeden, R. P. A., 559(56) (2) , 218(2, 55), 220(2, 55), 240, 242 Sutton, L. E., 338(30), 389 Swallow, A. J., 318(96, 97), 319(97),

Snook, G. F., 26(9), 102 Sobel, H., 250(36), 288 Song, P. S., 422(101), 426(101), 430 525, 376(91, 92), 391

Swanwick, M. G., 253(55), 288 Sweany,R. L.,512(51),537 Swenson, C. A., 259(86), 306(55), 307

Songstad, J., 250(36), 288 Sorrell, T., 59(85), 85(85), 86(85),

105 Spallo.C, 110(2), 120(2), 141, 152(26), (55), 310(55), 313(55), 522, 527(114),

154(26), 165 Sparks, R. A., 26(16, 17, 18), 40(16),

559, 549(15), 579 Symons, M. C. R., 338(34), 559 Szeverenyi, Z., 248(23), 252(47, 51,52), 103, 234(17), 240, 342(44), 389, 422

(100), 430, 467(9), 472(9), 482(9), 253(23,47), 257, 255 498

Spears, C, 156(51), 166, 250(33), 287 Sperati, C. R., 404(35), 406(54), 418

Tachkova, E. M., 255(78), 259, 513(58), 557

(35), 428 Spiller, R. C., 24(3), 25(3), 102 Spiro, T. G., 343(56, 57), 344(56), 390 Sprinson, D. B., 149(16), 164 Srivastava, R. C, 438(12a), 461 Stadlbauer, E. A., 527(116), 539 Stadtman, E. R., 151(20), 165, 532(139,

Tackett, S. L., 252(41), 254(41), 255, 418(88), 419(88), 430

Tada,M., 317(89), 525 Taft, R. W., 259(84) Tait, A. M., 250(32), 257 Takach,N. E., 706(118) Takahashi, K., 150(19), 161(91), 764 Takahashi, T., 115(19), 133(19), 742 Takeuchi, S., 89(115), 106 Tamao, Y., 451(40), 462 Tanchiang, Y.-T., 497(52), 500 Tani, M. E. V., 706(110) Tanzher,G., 317(90), 525 Taube, R., 335(18), 559 Tauzher, G., 256(91), 270(91), 277(171),

140), 540 Stadtman, T. C, 147(8), 155(8), 164,

528(120, 121), 529(120), 539, 574 (80), 581

Stafford, W. S., 230(79), 234(79), 242 Stahlberg, K.-G., 147(6), 164 Steen, V. D., 156(53), 166 Steeples, I. P., 285(204), 286(204), 294 Stefani, L., 256(91), 270(91), 277(170, 280(91), 290, 292, 336(24), 559, 502

171), 280(91), 290, 292, 336(24), 389, (3) , 514(3), 555 Taylor, L. T., 252(40), 255 Taylor, R., 706(117), 266(106, 107),

502(3), 514(3), 535 Steggles, P. N , 525(100), 526(100), 539 Stephens, R. S., 559(104) Stephenson, G. F., 125(50), 143, 204

290 Taylor, R. T., 162(73, 74), 766, 527(38),

404(32), 405(32), 418(32), 425, 524 (92), 528(122, 123), 555, 540

(13), 240 Stephenson, J. R., 112(14), 113(14),

H4(14b),742 Sternlicht, H., 489(42), 500 Stoeckli-Evans, H., 33(38), 103, 223(67),

Taylor, S. E., 468(12), 499 Tezuka,M., 300(17), 520 Thachuck, R. D., 482(24), 487(24), 488

(24), 489(24), 493(24), 497(24), 499

224(67), 242, 342(46), 390 Stothers, J. B., 144(63) Stotter, D. A., 266(106, 107), 290, 539 Thomas, R., 125(50), 744, 222(66), 242

Trkula,M., 85(89), 105 Trotman-Dickenson, A. F., 531(133), 540

Thompson, M., 122(43), 123(43), 125 (43, 51), 126(51, 53), 129(43, 56), 130(56), 132(60), 133(60), 135(43, 60), 143,144 Trueblood, K. N., 26(12, 15, 16, 17, 18,

20), 28(26), 40(16), 102, 103,106 (121), 110(7), 747, 202(1), 204(1, 10), 205(16), 234(17), 240, 342(44), 389, 422(100), 430, 467(9), 472(9), 482 (9), 498

Thomson, A. J., 401(17), 402(17), 403 (17), 422(17), 426(17), 427

Thornton, J., 456(5), 467(5, 7), 468(7), 469(7), 471(7), 472(7), 473(5, 7), 482 (7) , 483(7), 484(7), 492(7), 493(7), 494(7), 496(5), 498 Tsou, D., 512(52), 537

Thorp, R. G , 255(81), 289, 329(1), 333 Tucker, S. P., 270(144), 271(144), 275 (144), 297 (I) , 336(27), 343(52), 346(52), 347

(52), 348(52), 349(52), 350(52), 351 (52), 354(52), 362(52), 369(52), 388, 389, 390, 397(8), 404(22, 27, 28), 408

Turner, A. M., 456(5), 467(5, 7), 468 (7), 469(7), 471(7), 472(7), 473(5, 7), 482(7), 483(7), 484(7), 492(7), 493 (7), 494(7), 496(5), 498 (8) , 409(8), 412(27, 67), 427, 429, 468

Tyagi,S., 485(34), 499

(10) , 482(29), 484(29), 487(29), 488 (29), 490(29), 491(29), 498, 499

Udenfriend, S., 426(106), 430 Ueda,T., 300(17), 320 Ugi, I., 255(76), 261(76), 289, 523(87), 538

Tinker, H. B., 518(77), 538 Titchmarsh, D. M., 256(93), 257(93),

261(93), 263(93), 265(93), 266(108), 267(108), 290

Tkachuck,R. D., 268(126), 291 Tobe, M. L., 256(90>, 289 Todd, A. R., 110(5,7), 120(5),

Umani-Ronchi, A , 377(96), 597, 545 (4) , 558( 4), 57 7(4), 578

Umetani,T., 311( 65), 52 2 Umrikhina, A. V., 121(42), 122(42), 141, 202(2), 204(2, 11), 215(2,

745 11), 218(2, 55), 220(11,55), 225 Urry,W. H.,540 Ushio, K., 306(51), 527

(II) , 226(11), 227(11), 230(79), 231(11), 234(79), 236(11), 238 (11) , 240, 242, 417(81), 418(80), 429 Valiant, J., 26(8), 102

Valinsky, J., 68(57), 104, 461(29), 545 Tom, G., 517(75), 538 (5) , 578 Toohey, J. I., 147(2), 156(47), 164,

Valinsky, J. E., 382(121), 592, 451 (36, 37), 462, 547(6), 558(47), 559(47), 578, 580

165, 207(23), 211(23), 240, 306 (52), 321, 397(7), 401(7, 16), 403 (7), 405(7), 422(7, 16), 427

Topich, J., 515(70), 516(70), 517(69), van den Bergen, A., 525(96), 539 van den Broek, P., 245(100) 535(70), 538

Toraya, T., 65(56), 104, 306(51), 321, Vanngard,T., 437(11), 467 Vanston, N. J., 314(78), 522, 412(71),

429 579(11)

Toscano, P. G., 85(87), 705 Toscano, P. J., 86(95), 105, 359(72), 375 Van Voert, H. C, 409(62), 429

Veer,W. L. C, 404(44), 428 Veillard, A., 396(4), 398(4, 15), 400 (15), 411(15), 419(15), 427, 530(131), 540, 556(38), 562(38), 564(38), 576 (38), 579

(72), 382(72), 597, 505(18, 20), 506 (20), 531(18, 20), 536

Townscnd,C. A., 112(13), 113(16), 115 (7), 117(26), 120(26), 142, 218(52), 241, 473(19), 479(19), 480(19), 481

Venerable, G. D., 253(54), 288, 506(23), (19), 499 Toxano, P., 491(47), 500 Toy, A. D., 438(126), 461 Trimm, D. L., 428

514(23), 536 Venkatesan, K., 33(36, 37), 103, 205(15),

207(15), 240, 342(47), 344(47), 347 (47), 390 Trivedi, B. K. , 377(99), 37 9(99), 392,

567(62), 580 Verenikina, S. G., 267(109, 110), 290

Waters, J. M., 33(34), 103, 33(34), 78 ( 1 2 ) , 103, 105

Vergamini, P. J., 301(24), 304(24), 320, 354(70), 391, 404(31), 418(31), 428,

Waters, T. N., 78(72), 105 492(46),500, 552(20),579 Vickery, T. M., 258(96), 282(191), 293, Waters, T. N. M., 33(34), 103

Watson, C. J., 116(23), 142 297(5), 307(5), 316(86), 320, 323, Watson, W. P., 284(198), 293, 532(136,

137, 138), 534(149), 540, 541, 571 (73), 572(74), 575(73, 75), 581

575(88), 581 Viennet, R., 420(99), 430 Vitols, E., 159(62, 63), 161(63), 166,

Weber, H., 144( 1 0 ) 449(34), 461 Vitols, V. S., 163(82), 167 Vlcek, A. A., 252(48), 288, 335(15),

Weber, J. H., 262(103), 263(103), 290, 525(93), 527(113), 538, 539, 571(70), 581 389

Webster, J. R., 567(59), 580 Vogelman, H., 110(2), 120(2), 141 Weijel,M., 428(49)

Vogelmann, H., 230(82), 231 Weissbach, H., 147(1, 2), 156(44, 47, 49, 50), 159(49), 162(73, 74), 163 (50, 79, 84), 764, 765, 766(51), 767, 254(71), 289, 296(2), 312(73), 319, 321, 331(9), 367(9), 528(122, 123), 540

(82, 84, 89), 238(82), 243 Volcani, B. E., 156(47), 165, 296(2),

312(73), 319, 321 Volpin, M. E., 516(72,1 3 ) , 538 von Deuten, K., 92(127), 106 von Schlingmann, G., 40(47), 104 Werthemann, L., 69(58, 59), 104, 236

( 9 1 ) , 243, 538 West, B. O., 525(96), 539 West, P. R., 573(79), 581 Westrum, E. F., 509(43), 537 Weyhenmeyer, R., 110(3), 120(3),

Wade, R. S., 522(86), 538 Wagner, F., 72(60, 61), 104, 110(2), 120

(2), 141, 148(14, 15), 151(21), 152(15, 25), 154(25), 155(15), 164, 165, 211 (29, 30), 216(42, 44, 46), 217(42, 48), 226(42, 44, 46), 230(82), 231(34, 83, 89), 235(91), 238(82), 241, 243, 278 (174), 292, 298(7), 320, 417(79), 429

747 White, H. A., 576(91), 582 White, J. G., 26(11, 12, 15, 17, 18,20),

28(25), 102, 103, 110(7), 747, 202(1), Wagner, H. A., 152(28), 765 204(1, 10), 205(16), 240, 342(44), Wahl, D., 235(91), 243 389, 422(100), 430, 467(9), 472(9), Walerych, W., 154(38, 39), 765(41), 230

(81), 242 482(9), 498

White, R.C., 426(105), 430 Whitear, B. R. D., 300(21), 303(21), 320, Walker, G. A., 157(57, 59), 158(57), 159

(62,63), 161(63), 766 Walker, T. E., 268(127, 128, 129), 297,

335(22), 389, 404(34), 405(34), 418 (34), 428

Whitcsides, G. M., 260(99), 290 Whitlock,H., 125(50), 143 Whitman, P. J , 112(13), 742, 473(19),

313(76), 322, 478(21), 486(36), 488 (21), 489(21), 490(21), 493(48), 495 (21, 51), 497(51), 499, 500

Walling, C, 532(134), 534(134), 540, 479(22), 480(19), 481(19), 499 Wick, A., 247(39) Widdowson, D. A., 317(91), 323 Wijmcnga, H. G., 404(44), 428 Wild, H., 202(5), 209(5), 212(5), 214

556(44), 580 Wallis,0. C, 576(91), 582 Walters, W. A., 252(55), 288 Waltzman, R., 280(180), 293 Wang, D. M., 575(90), 582 Ward, B., 404(22), 427 Ward, D., 281(185, 186), 293, 549(1 3),

(5), 217(5), 227(5), 230(5), 240 Wilkinson, G., 276(160, 162), 292, 340

(40), 389 Williams, D. A., 260( 100), 290, 539 Williams, D. C, 115(18), 116(25), 117

578 Watanabe, E., 246(4), 254(62), 255(62),

256(62), 257(62), 263(62), 265(62), 286, 289

(25, 31, 32, 33), 118(33), 120(25b), 122(43), 123(43), 125(43), 129(43),

Watenpaugh, K., 404(25), 427 135(43), 742,143

Williams, F. R., 255(82), 289, 527(112), 539

Wolf, D. E., 26(8), 102, 110(6), 141, 239(104), 243

Wolfe, R. S., 303(35), 321,490(43), Williams, J. R., 404(22), 427 Williams, R. J. P., 255(81, 82),

289, 311(69), 312(69), 314 (78), 322, 336(27), 338(32), 339 (32), 343(52, 53), 345(59), 346 (52), 347(52), 348(52), 349 (52, 53), 350(52), 351(52, 59), 353(59, 66, 67), 354(52), 362 (52), 369(52), 389, 390, 391(75), 394(1), 395(1), 397(8), 404(28), 407 (1), 408(8), 409(1, 8, 60, 61), 412(60, 67, 71), 413(61), 415(61), 418(68, 85), 420(1, 68), 422(1, 68), 427, 429, 430, 451(38), 452(38), 456(5, 6), 458(57), 462, 464(2, 3, 4), 467(5, 7), 468(7, 10, 11), 469(2, 7, 11), 471(3, 7), 472 (7), 473(5, 7), 482(7, 29), 483(7), 484 (3, 7, 29), 487(3, 29, 40), 488(29), 490 (2, 29, 50), 491(29), 492(7), 493(7), 494(3, 7), 495(50), 496(5), 497(50), 498, 499, 500, 527(110,112), 539, 558(48), 580

500 Wong, L. Y., 256(90), 264(105), 289,

290, 518(79), 538 Wood, J. M., 291(119, 120), 298(10),

303(35, 36), 30 7(59), 312( 70), 320, 321, 322, 405(45), 428, 432(4), 449 ( 4 ) , 460, 469(15), 486( 35), 49 0(43, 50), 495( 50), 49 7(50, 52) , 499, 500, 504(7), 517( 76), 526( 105), 52 8(7), 529(105), 535, 538, 539

Wood, T. R., 25(5), 102, 239(104), 243

Woods, D. D., 147(5), 164, 529(124, 125), 540

Woodward, R. B., 169-200, 202(5), 209(5), 212(5), 214(5), 217(5), 227(5), 230(5), 240, 498(53), 500

Worner,G., 117(30), 143 Wozniak, W., 343(56), 344(56), 390 Wurziger, H. K. W., 117(31, 32, 33), 118

(33), 121(41), 143 Willis, B. T. M., 313(75), 322 Wilson, M. R., 156(47), 165 Ya Bykhovsky, V., 132(60), 133(60), Wilt, J. W., 379(110), 392, 556(35),

579 135(60), 144

Yacynych, A. M., 85(90), 105 Yagen,B., 116(24), 142 Yakovlev, V. A., 267(116, 117), 285

Windgassen, R. J., 158(61), 166, 240, 247(8, 9), 250(30), 252(9), 253(30, 56), 256(8, 88), 257(94, 95), 258(97), 269(8), 283(88), 287, 288, 289, 290, 300(22), 301(22), 302(22, 31), 303 (22), 304(40), 307(58), 311(58, 66), 312(58), 313(31), 314(31), 320, 321, 322, 404(30), 418(30), 419(30, 95), 427, 430, 507(33), 508(36), 518(78), 524(33, 36), 525(33), 527(115), 529 (115), 536, 538, 539

(117), 290 Yakusheva, M. I., 267(111), 290 Yamada, R., 253(57), 268(124), 288, 291, 301(25), 302(30), 311(65), 320, 321, 322, 432(3), 433(3), 439(3), 441 (3), 442(3), 449(3), 460, 508(38), 522 (84), 524(38), 525(38), 536, 538

Yamaguchi, K., 556(39), 580 Yamano, Y., 406(55), 419(55), 428 Yavorskaya, A. N., 121(42), 122(42), 143

Winficld, M. E., 277(167), 292, 432(2, 3), 433(2, 3, 9), 434(9), 437(9), 439 (3, 9, 21), 440(9), 441(3), 442(21), 443(3, 21), 444(21), 445(21), 449(3, 21), 453(9), 457(9), 458(56), 460, 461, 462

Yoshida, Z ., 246( 4), 254( 62), 255( 62), 256(62), 257( 62), 263( 62), 265( 62), 286, 289

Yoshizawa, J., 295(181) Winnacker, E. L., 214(41), 241(39) Yurkevich, A. M., 255(78), 267(109,

110, 117), 282(189), 284(199, 200, 201, 202, 203), 285(117, 200, 202), 289, 290, 293, 294, 298(8, 12), 299 (12), 305(49, 50), 306(49, 50), 320, 321, 363(80, 81), 391, 513(58), 537, 549(14), 5 7 3(77), 575(85), 5 78, 581

Wintner,C. E., 78(75), 105 Wise, I. J., 161(69, 70), 166 Witkop, B., 228(70), 242 Witman,M., 525(93), 538 Witman, M. W., 527(113), 539 Woggon, W.-D., 132(60), 133(60), 135

(60, 66), 144

Subject IndexAbbreviations, nomenclature, 20 Absolute configuration: 3-episirohydrochlorin, 130 vitamin B12, 28 Acetaldehyde: [2-2H,3H]acetaldehyde from ethanolamine, 558 e hanolamine, vitamin B1 2 coenzyme

photolysis, 298 2-ethoxyethylamine, vitamin B12 coenzyme photolysis, 298, 328 ethylene glycol: pulse radiolysis, 574 vitamin B12 coenzyme photolysis, 298

methyl(aquo)cobaloxime photolysis, ethylene glycol, 571 Acctamide side chain, vitamin B12, 30 Acetic acid, carbon dioxide reduction,

528 Acetoin, vitamin B1 2 total synthesis,

172 Acetone:

bis(salicylaldehyde)ethylenediiminecobalt(lII)(CH3OH),alkylation, 518

cobalt alkylation, 280 cobalt(III) complexes, alkylation, 517 photolysis, /3-hydroxypropylcobaloximes,

302 reaction with aquohydroxo Co(III),

336 Acetonitrile formation, methylcobaloxime

and cyanide, 307 2-Acetoxyalkylcobaloximes: conversion to: 2-alkoxyalkylcobaloximes, 575 olefin 7r-complexes, 575 preparation, 284

2-Acetoxyethyl(pyridine)cobaloxime, 13C-Iabelled, 534

Acetylcobalamin: alkali, vitamin B12, 311 reaction with hydroxylamine. 312 Acetylene: addition to cobalt(I) complexes, 256

carbanion reaction with cobalt(III) complexes, 279

pentacyanocobaltate, reaction with, 276

Acetylglycobalamin, reaction with hydroxylamine, 312

Achlorohydria, 1 Acid catalysis: alkylcorrins, decomposition, 369 2-hydroxyethylcobaloxime, olefin

7r-complcxes, 575 phenacylcobalamin, olefin n-complexes, 575

Acid catalyzed decomposition isopropylcobalamin rate, 371

Acid catalyzed rearrangement to 0-hydroxy- ft-propylpyridinatocobaloximc, |3-hydroxy-isopropy lpyridinato-

cobaloxime, 314 Acid catalyzed,electrophilicdecomposition: alkylcobalamins, 527

2-hydroxyethylcobaloximes, 518 Acid cleavage:

adenosylcobaloxime, 312 adenosylcorrinoids, 312 Coa-adenyl-Co|3adenosy lcobalamin, 312 3-isoadenosylcobalamin, 312

Acid decomposition: 2,3,dihydroxy-4-pentenal, vitamin B12

coenzyme, 312 cobalt-carbon bond, vitamin B1 2

coenzyme, 366

Acid decomposition (Cont'd) b-ethoxyctIiy 1(pyridine) cobaloximc, ethylene, 313 ethylene, hydroxyethylcobalaniin, 313 methoxyethylcobalamin, ethylene,

313 Acid hydrolysis: nucleotide loop, 234 vitamin B12: chromatography, 230 cobyrinic acid, 230, 232, 234 Acidity: hydridocobalt complexes, 253, 506 hydridopentacyanocobalt, 252 Schiff-base complexes, 506 vitamin B1 2S, 253 Acrylate radical, vitamin B12 coenzyme, glutainate mutase, 571 Acrylonitrile: addition to cobalt(I) complexes, 256

olefin p-complexes, cobalt(I) complexes, 527

Activation, corrin ring, S-adenosylmethionine, 345 methionine synthetase, 162 Activation enthalpy: homolytie cleavage, cobalt-carbon bond, 511

kine ics, cobalt-carbon bond, 5 1 1 1-phenylethylcobaloximes, axial ligands, role, 5 1 1

Active site thiol, vitamin B12 coenzyme, enzymic reaction, 555

1-Adamanthyl( pyridine)cobaloxime, preparation, 255

Addition of chlorine, vitamin B12, 216

Addition of guanosine diphosphate, cobinamide phosphate, 151

Addition of lower base, cobalamins, biosynthesis, 153

Addition to: cobalt(l) complexes: acetylene, 256 acrylonitrile, 256 alkynes, 256 mechanism, olefins, 262 olefins, 256

3,3,3-trifluoropropyne, 257 corrin, conjugated system, 238

olefins, mechanism: cobaloximes, 264 cobalt(I) complexes, 265 hydridocobalt complexes, 265 hydridopentacyanocobalt,

263 unsaturated electrophiles, cobalt(I) complexes, 256 Adenosine-5 -carboxaldehyde, 363 formation, 297 structure, 297 Adenosine triphosphate, vitamin B12

coenzyme, biosynthesis, vitamin B1 2 523 Adenosylating enzyme: metal ions, 161 nucleoside triphosphates, 160 Adenosylation: C. tetanomorphnm, table, nucleoside triphosphates, 160 corrin, 155 Adenosyl carbene, vitamin B1 2 coenzyme, 549 Adenosylcobalamin, see Vitamin B12

coenzyme Adenosylcobalamin-agarose, affinity

chromatography, 268 ara-Adenosylcobalamin, reac ion with

cyanide, 306 L-Adenosylcobalamin, reaction with

cyanide, 306 Adenosylcobaloxime: acid cleavage, 312 reaction with, alkali, 307 Adenosylcobinamide, 155 Adenosylcobyric acid, 155 Adenosylcorrinoids, acid cleavage,

312 S-Adenosy homocysteine, 363 S-Adenosylmethionine: activation, corrin ring, 345 methionine formation, 329 Coa-adenyl-Co/b-adenosy lcobalamin, reaction with cyanide, 305 Adenylcobamide, coordination chemistry, 351 AdoCbl, see Vitamin B1 2 coenzyme Adocobalamin, see Vitamin B12 coenzyme Aerobaetcr acrogenes, cobalamin

biosynthesis, 160 Affinity chromatography: adenosylcobalamin-agarose, 268

Affinity chromatography (Cont'd) corrin, 268

ribonucleotide reductase, 268 Aggrega ion, cobalamins, 491 Air dried crystals, vitamin B12, 25 Alkali:

adenosylcobaloxime, 307 reaction wi h alkylocobalt complexes, 307-311 vitamin B12, cobalt, reduction by,

226 vitamin B12s, acetylcobalamin,

311 Alkaline decomposition:

cobalt-carbon bond, vitamin B12

coenzyme, 366 cyanocthylcobalamin, 366 ethoxycarbonylcobalamin, 360 Alkaline phosphatase: cobalamin phosphate, dephosphorylation, E. coli, 155 2-Alkoxyalkylcobaloximes, 2-acetoxyalkylcobaloximes, conversion to, 575 Alkylating agents, cobalt complexes, 254 Alkylation: acetone, bis(salicylaldehyde)ethyIene- diiminecobalt(III)(CH3 OH), 518 cobalt(III) complexes, 517 alkyl halides: cob(I)aloximes, 523 cobalt(I) complexes, 523 cobalt(II) complexes, 518 tricyclohexylphosphinecobal(II)oximes, 519

vitamin B12r, 520 vitamin B12s, 523 alkyl iodides versus other alkyl halides, cobalt(Il) complexes, 522 alkylcobaloximes, mercury(ll), 526 alkylcobalt complexes:

arsenic(III), 526 mercury(II), 526

thallium(III), 526 axial ligand effects, cob(II)aloxirnes, 519 cobalt(I) complexes, stereochemistry,

vinyl halides, 260, 502 cobalt(III) complexes, cobalt-carbon

bond formation, 517-524 corring, 214 CoTPP, disproportionation, 279

diazoalkanes: cobalt(III) complexes, 281

cobalt porphyrins, 281 electron transfer, cobalt(I) complexes, 259 gold(I), alkylcobalt complexes,

527 Grignard reagent, cobalt(III) complexes,

277,517 hydrazines and oxygen:

cobaloximes, 275 cobalt complexes, 275

kinetics, table: cobaloximes, 259 cobalt(I) complexes, 258 mercury(II),

vitamin B12S, 259 mercury(II), methylcobalamin, 526 metliylpentacyanocobaltate(III), mercuric

chloride, 526 nitromethane, cobalt, 280 olefin addition: cob(I)aloximes, 523 cobalt(I) complexes, 523 organolithium reagents, cobalt(III)

complexes, 517 palladium(II), alkylcobalt complexes,

527 pentacyanocobaltate, 502 platinum(IV), alkylcobalt complexes, 527 radical intermediates:

bis(salicylaldehydc-o-phenylenediiminecobalt(II), 518

cobalt(II) complexes, 518 vitamin B121-, 520

stereochemistry: cob(I)aloximes, 523 cobalt(I) complexes, 523

vitamin B12S, 260, 523 synthetic utility, vitamin B121-, 277 tin(IV), alkylcobalt complexes,

527 trans-dimethylcobalt(III) complexes: cadmium, 527 lead(II), 527 zinc(II), 527 vinyl e hers: cob(III)aloxime, 281 hydroxocobalamin, 281 Alkylcarbinylcobalamin, 362

Alkylcobalamins: acid catalyzed electrophilic decomposition, 527 alkyl reactions, 295-323 base-on, off, photolability, 303 bond dissociation energy, 513 cobalt-carbon bond thermolysis, 525 conformations, 341 5- and 6-coordinate, 346, 351 dealkylation by thiols, 527 c/s-diaminoplatinum(II) coordination, 495 five coordinate, decomposition, 369 heterolytic cleavage, 305-319 13C-Iabelled, 268 nomenclature, 21 one-electron oxidation, 517 photolability, 524 photolysis, role of, O2, 366 vitamin B128, formation, 300-303 pK values, benzimidazole, table, 351, 494 protonation, table, 35 1 quantum yield, photolysis, 303 rate of decomposition, 365, table, 368 reaction with:

acid, 313 cyanide, 306

steric effects: ligand exchange, 341 on structure, 341

thermolysis, 303 thiols, 527 very strained, rate of decomposition,

371 vitamin B12r, reductive cleavage,

317 see also Alkylcobalt complexes; Cobalt complexes; Cobalt-carbon bond; Me hylcobalamin; VitaminB12

coenzyme Alkylcobaloximes: alkyl ligand reactions, 295-323 axial Ugand exchange rates, 248 cation radicals, epr spectrum, 515, 517 chromatography, 247 cobalt-carbon bond length, 359 crystallization, 248 dealkylation, thiols, 527 electrochemical oxidation, 515 electronic spectrum, 406 b-elimination, 364

halogen cleavage, 317 heterolytic cleavage, 305-319 hexachloroiridate, oxidation, table, 516 mercury(II), alkylation, 526 oxidation, one electron, 515 photolysis:

epr spectroscopy, 525 quantum yield, 300-303, 364, 525

pyridine complexes, hydrolysis, 248 reaction with mercaptides, 311 redox chemistry, 515 redox potential, 516 thermolysis, 303, 364 X-ray crystallographic data, 80 X-ray structure, 359 see also Alkylcobalt complexes (Alkylcobalt)+, nuclcophilic displacement,

R+ from, 516 Alkylcobalt complexes: alkylation:

gold(I),527 palladium(II), 527 platinum(IV), 527 tin(IV), 527

alkyl reactions, 295-323 arsenic(III), alkylation, 526 bond dissociation energy, Schiff-base

complexes, 5 1 2 cobalt-carbon bond:

length, table, 505 thermolysis, 525

flash photolysis, 525 formal oxidation state, 514 5,7,7,1 2,14,14-hcxamethyl-l,4,8,11- tetraazacyclotetradeca-4,11-dienecobalt, 271 ligand modification, 283-286 mercury(Il):

alkylation, 526 stereochemistry, 526

model systems, vitamin B12 coenzyme, 551,564

photolability, 553 photolysis:

anaerobic, 553 bis(acetylacetone)ethylenednminecobalt,

524 bis(salicylaldehyde) ethylcnediimine-

cobalt complexes, 524 diacetylmonoximcimino diacetylmono-

ximatoiminopropane-1,3-cobalt(I), 524

1,4,8,11-tetraazacyclotetradecane, 524

Alkylcobalt complexes (Cont'd) quantum yield, 553 radical traps, 553 spin-traps, 524, 552 reaction with tetracyanoethylene, 285 redox chemistry, diacetylmonoximeimino diacetylmonoximatoiminopropane- 1,3-cobalt, 514 thallium(III) alkylation, 526 1,4,8,11-tetraazacyclotetradccane, 524 thermolysis, 552

transalkylation, cobalt(I) complexes, 527 see also Cobalt-carbon bond Alkylcobalt(IV) complexes, SchifT-base

complexes, 516 Alkylcobinamides: electronic spectrum, temperature variation, 348 pH decomposition rates, 370 Alkylcorrins: cobinamides cobalamins, 369 decomposition, acid catalysis, 369 imidazole coordination, 358 olefins decomposition, 365 photoaquation, 301 photolysis, olefins, 302 Alkyl halides: bis{ 1,2-cyclopentanedioximato) cobalt, cobalt(II) complexes, reaction with, 274

bis(salicylaldehye-o-phenylenediiminecobalt) Co, cobalt(II) complexes, reaction with, 274 cob(I)aloximes, alkylation, 523 cobalt(I) complexes, alkylation, 523 cobalt(II) complexes:

alkylation, 518 halogen abstraction, 519 reaction with, 273 reactivity towards, 521

pentacyanocobaltate: olefins from 519 reaction with 274

reactivity towards: bis(salicylaldehyde-o-pheny lenediimine-

cobalt(II) (py), 521 pentacyanocobaltate, 521 triphenylphosphine cob(II)aloximes, 521 vitamin B12r, 521

1,4,8,1 1-tetraazacyclotetradecane: cobalt(II), reaction with, 274 tricyclohcxylphosphinecobal(II)oxime, alkylation, 519

vitamin B12r: alkylation 520 reaction with 274 vitamin B12S, alkylation, 523 Alkyl iodides, cobalt(II) complexes, alkylation, 522 Alkyl ligands: cobaloximes, optically active, 268

effect on physical properties, table, corrin, 356 electronic spectrum, effect, 356 pK values, effect, 356 reactions, 295-323 Alkylperoxocobalt complexes, 55 3 Alkyl(pyridine)cobaloximes, cation exchange resin, hydrolysis, 249 Alkyl radicals, cobalt, recombination with, 335 Alkyl reactions: alkylcobalamins, 295-323 alkylcobalt complexes, 295-3 23 Alkynes: addition: cobalt(I) complexes, 256 mechanism, 263 stereochemistry, 256 Alkynylcobalt complexes, synthesis, 279 Amide activation, vitamin B12, total synthesis, 192 f-Amide cleavage, group participation

effects, 231 Amide dcamination, vitamin B12 total

synthesis, 191 Amide groups (corrin periphery): hydrolysis: acid, 230 base, 234 rates of hydrolysis, steric, 231 vitamin B12 hydrolysis, side chain,

33 Amide hydrolysis, dinitrogen tctroxide.

VitaminB total synthesis, 192 12Amide side chain, nomenclature, vitamin

B12, 19,30 Aminoalcohols (vicinal), radical rearrange-

ments to aldehydes, 573

Aminocobalamin, electronic spectrum,

411 10-Aminocabalamin,217 8-Aminocobyrinic acid abcdefg-hexamcthyl ester c-lactam, preparation, 236

Apoenzyme, circular dichroism, binding of corrin, 423

Coa-aquo-Co/3-adenosylcobamide, reaction with cyanide, 306 Aquocobalamin, circular dichroism, 420 electronic spectrum, 417 enzymic reduction, 157 ligand substitution, equilibrium constants, table, 337

nmr spectrum, praseodymium, 468, 474, 483

pulse radiolysis, 318 reaction with: malononitrile, 279 phenylacetonitrile, 279 redox potential 5 14 see also Cobalt complexes; Hydroxo- cobalamin Aquocob(II) inamide:

epr spectrum, 448 Aquocyanocobinamide, electronic spectrum,

408, 413 Aquocyanocobyric acid: bond lengths, 206 structure, 205 Aquohydroxo Co(III): acetone, reaction with, 336 nitromethane, reaction with, 336 Aquohydroxocobinamide, electronic- spectrum, 413 Aristeromycyclocobalamin : photolysis, 297 reaction with: cyanide, 306 hydroxide, 307 Arndt-Fistert, vitamin B12 total synthesis, 194 Aromaticity: corrin, 204 vitamin B12 204 Arsenic(IH) alkylation, alkylcobalt complexes, 526 Arylcobaloximes, 271 Aryl cobalt complexes, bis(acetylacctonc) ethylenediiminecobalt, 275 Aryl halides, vitamin B12s, reaction with, 271 10-Aryloxycobalamin, 217 Ascorbic acid:

role in formation, yellow corrinoids, 39 vitamin B12, reaction with, 229 yellow corrinoids, 229

8-Aminocobyrinic acid c-lactam dicyanide, see Hcxacarboxylic acid, vitamin B12

/3-Aminoethylcobalt complexes, preparation, 257

2-Amino-2-hydroxy radical, 558 5-Aminolevulinic acid, incorporation into,

corrin, 111 [5-13C]-aminolevulinic acid, vitamin B1 2,

biosynthesis, 479 2-Aminomebularine, vitamin B12 coenzyme,

fluorescent analogs, 300 Aminome hylbilanes: corrin biosynthesis, 117 deamination, 118

porphobilinogen deaminase, deamination, 117

structure, 11 8 Aminomutases: enzymic reaction, 546 MO calculations, 557 model systems, vitamin B12 coenzyme, 571

pyridoxal phosphate, 329 radical intermediates, 556 reaction pathways, vitamin B12 coenzyme, 573

2-Amino-l-propanol, radical intermediates, enzymic reaction, 450

[R] -l-Amino-2-propanol: nucleotide loop, biosynthesis, 149 phosphorylation, 151 synthesis, 1 3

L-threonine, conversion to, 199 threonine decarboxylation, 150 Anaerobic photolysis, alkylcobalt complexes, 55 3 Analogs, vitamin B12 coenzyme, 551 Analysis of reaction mixtures, cobalt- carbon bond synthesis, 247 [14] Ane HA, see 1,4,8,11-Tetraaza-

cyclotetradecane Angular anomalies, cob(II) inamides, epr spectroscopy, 443 4',5'-Anhydroadenosine, 549 Animal protein factor, vitamin B12, 14 m-Anisidine, vitamin B12 total synthesis, 172 Anisotropic hyperfine interaction, cob(Il)

inamides, epr spectroscopy, 443 Anomalous dispersion. X-ray structure,

97 Antipernicious anemia factor, vitamin B12,

11

Assay, vitamin B12 coenzyme, biosynthesis, vitamin B12S, 159

Atrophic gastris, 1 Axial ligand effects, cob(H)aloximes, alkyla-

ion, 518 Axial ligand exchange rates, alky lcobal-

oximes, 248 Axial ligands:

cobalt-carbon bond, bond dissociation energy, 531

equilibria, 345 role, activation enthalpy, 1-phenylenthyl- (pyridine)cobaloxime, bond dis- asssociation energy, 510 steric requirements, corrin, 255 vitamin B12 coenzyme constraint of, 41 5- and 6-coordinate corrin, 346 Axial phosphincs bond lengths, cobaloximcs, 83 Azidocobalamin, electronic spectrum, 411,

417 Azidocob(ll)inamide, epr spectrum simula-

ion, 445

B12 coenzyme, see Vitamin B12 coenzyme B12r, see Vitamin B12r

B12 s> see Vitamin B12 s

7-Band, electronic spectrum, effect of axial ligands, 411, table

Base-on, off: electronic spectrum, vitamin B12

coenzyme, 357 epr spectrum, vitamin B121-, 299 isopropylcobalamin, thermolysis, 552 photolability, alkylcobalai.iins, 303 vitamin B12 coenzyme, 350

Beckmann rearrangement, vitamin B12

total synthesis, 180 Benzimidazole:

alkylcobalamins, pK values, 351 effect on corrin ring folding, 59 pKa values when coordinated, 54 vitamin B12 coenzyme pK values, 351

/V-Benzoyladenosylcobalamin, reaction with cyanide, 306

Benzoyl! 1-pyridine) methanide(chloro)- cobaloxime, preparation, 276

Benzyl bromide: reaction with: vitamin B12 r , 5 1 3 vitamin B12 s, 51 3 Benzylaquocobaloximc, redox potential, 516

Benzylcobalamin, stability, 255, 513 Benzylcobaloxime, halogen cleavage, 317 Benzylcobalt complexes, thermal stability, 513 Benzylcobalt(octaethylporphyrin), stability,

255 Bilanes:

aminomethyl: corrin biosyn hesis, 117 deamination, 118 hydroxymethyl, corrin biosynthesis, 118 1-methyl, corrin biosynthesis, 121

Binding of corrin to apoenzyme, circular dichroism, 423 Binding to apoenzyme, side chain modification, 65 Binding to ribonucleotide reductase,

Bnr, 442 Biological activity: lactams (corrin ring), 225 neocorrinoids, 8-epicorrinoids, 225 neovitamin B12, 224 Biosynthesis: addition of lower base, cobalamins, 153

Aerobaeter aerogenes, cobalamins, 160 [5-13CJ 5-aminolevulinic acid, vitamin B12, 479 [R]-l-amino-2-propanol, nucleotide

loop, 149 Clostridium stieklandii, cobalamins,

153 Clostridium thcrmoaceticum, methyl-

cobalamin, 161 cobalamins:

from cobyric acid, 148 nucleotide loop, 148

cobinamides, 151, 152 corrin, nucleotide loop, 107-144, 148 E. eoli, metliylcobalamin, 161 Euglena gracilis, corrin, 117 eukaryotes:

cobalt-carbon bond, 155 vitamin B12 coenzyme, 156

Factor I, 131 FMNH2 :

cobalamins, 148 methionine, 162 guanosinc diphosphate, nucleotide loop, 152 L. leichmannii, cobalamins, 160 Methanosarcina barkeri, metliylcobalamin, 162

Biosynthesis (Cont'd) [l 3CH3 ]-L-methionine, vitamin B12, 480 1-methylbilane, corrin, 121 methy lcobalamin:

mammalian, 163 methane, 161-163, 528

NADPH: me hionine, 162

methy lcobalamin, 162 nicotinate mononucleotides, cobalamins, 153 nmr spectroscopy, vitamin B12, 479 origin of carbon atoms, cobyrinic acid, 112 5-phosphoribosyl-l-pyrophosphate,

cobalamins, 153 [8-1 3 C] porphobilinogen, vitamin B12,

480 primary precursors, cobyrinic acid, 112 prokaryotes: cobalt-carbon bond, 155 vitamin B12 coenzyme, 156 Propionibacterium arabinosum, nucleotide loop, 152 Propionibacterium shermanii, corrin, 112 ribose-l-phosphate, cobalamins, 153 sirohydrochlorin, 123 Streptomyces griseus, methylcobalamin, 161 timing, cobalt-carbon bond formation,

155 trimethylated i sobacteriochlorins, 132 uroporphyrinogen(III) as precursor of

cobyrinic acid, 116 VitaminB12 coenzyme, 145-167 VitaminB12, 28, 107 vitamin B12s: adenosine triphosphate, vitamin B12

coenzyme, 523 assay, vitamin B12 coenzyme, 159 Biosynthetic studies, nmr spectroscopy, 486 Bis(acetylacetone)ethylenediamine, X-ray structure, complex with methylcobalamin, 349 Bis(acetylacetone)e hylenediiminecobalt(III), structure, 503 Bis(acetylacetone)ethylenediiminecobalt: alkyl complexes, photolysis, 524 aryl cobalt complexes, 275 bis(salicylaldehyde)ethylenediiminecobalt, redox potential, 504

pKa values, 504 l,l-Bis-(p-chlorophenyl)-2,2,2-trichloro- ethane, reaction with cob(I)aloxime, 266 Bis(l,2-cyclopentanedioximato) cobalt: cobalt(II) complexes, reac ion with alkyl

halides, 274 nucleophilicity, cobalt(I), 251 Bis(dimethylglyoximato) cobalt, see Cobaloximes Bislactone, sirohydrochlorin, 122 Bis(salicylaldehyde)ethylenediiminecobalt(II)(methylimidazole): halogen abstraction, electron transfer, 520 six coordinate, 519 Bis(salicylaldehyde)ethylenediiminecobalt(III): alkyl complexes, photolysis, 524 methyl complex, photolysis, 301 model systems, vitamin B12 coenzyme, 551

nucleophilicity, 523 propyl complex, photolysis, 302 reaction with carbanions, 279 redox potential, bis(acetylacetone)-

ethylenediiminecobalt, 504 structure, 552 vitamin B12 coenzyme, model systems,

551 7,7 '(CH3)2 bis(salicylaldehyde)ethylene-

diiminecobalt, pKa values, 504 Bis(salicylaldehyde-o-phenylenediimine)- cobalt, pKa values, 504 Bis(salicylaldehyde-o-phenylenediiminecobalt(II)(py): alkylation, radical intermediates, 518 alkyl halides, reactivity towards, 521 Bis(salicylaldehyde-o-phenylenediimine)- cobalt(III): cobalt(II) complexes reaction wi h alkyl halides, 274 redox potential, 504 structure, 503 Bond angles, distances, corrins, tables, 45-53 Bond dissociation energy:

alkylcobalamins, 513 axial ligands: cobalt-carbon bond, 531 role, l-phenylethyl(pyridine)- cobaloxime, 510 cobalt-carbon bond, steric effects, 507, 512

methyl(triphenylphosphine)cobaloxime,

cobalt-carbon bond, 505 nmr spectroscopy, methylcobalt complexes,

506 observed and ca lculated, corrin, 205,

table, 206 vinyl(pyridine)bis(salicylaldehyde)-

ethylenediiminecobalt, co balt- carbon bond,505

vinyl(pyridine)cobaloxime, cobalt- carbon bond,505

vitamin B12 coenzyme, cobalt-carbon bond,505 s-Bonded organocorrinoids, vitamin B12

sscoenzyme, enzymic reactions, sss547 p-Bonding, vitamin B12r, 440 Bond strength, vitamin B12 coenzyme,

cobalt-carbon bond, 513 Borohydride cleavage, carboxymethylcobalamin, 303 Bridged cation: diol dehydrase, enzymic reaction, 555 molecular orbitals, 555 theoretical studies, 557 Bridged cobaloximes, structure, 87, 269 Bridged dimers, cobaloximes, 268 Broken cell enzymes, corrin biosynthesis, 116 Bromination: corrin, 215 vitamin B12, 215 1 0-Bromocobalamin: acetylcobalamin, 411 axial ligands, table, 414, 415 chlorocobalamin, 411 preparation, 216 3-Bromopropylcobaloxime, thermolysis,

304 Buckling: corrin, 208, 342 vitamin B12, 208 But-3-enylcobalamin, cyclopropylcarbinylcobalamin, rearrangements, 567 But-3-enyl(pyridine)cobaloxime, cyclopropylcarbinyl(pyridine) cobaloxime, rearrangements, 568 But-3-enyl radical: cyclopropylcarbinyl radical rearrangements 557 t-Butylcobaloximes, 254

Bond dissociation energy (Cont'd) conforma ional changes, cobalt-carbon

bond,531 1-cyanoethylcobaloxime, cobalt-carbon

bond,511 equilibrium determination, 1-phenylethyl- (pyridine)cobaloxime, 508 hydridocobalamin, 507 hydridocobalt complexes, 506 hydridopentacyanocobalt, 507 hydrido(pyridine)cobaloxime, 507 hydrido( tri-w -b uty lphosphinc) cobaloxime, 507 isopropylcobaloxime, cobalt-carbon bond,

511 isopropyl(pyridine)bis(salicylaldehyde-o-

phenylenediimine)cobalt, 512 1-methyl-heptylcobaloxime,cobalt-

carbon bond,511 l-methyl-2-phenylethylcobaloxime,

cobalt-carbon bond, 511 neopentyl(pyridinc)bis(salicylaldehyde-o-

phenylenediimine)cobalt, 512 propyl(pyridine)bis(salicylaldehyde-o-

phenylenediimine)cobalt, 512 Schiff-base complexes, alkylcobalt com-

plexes, 512 steric effects, cobalt-carbon bond, 512,

531 vitamin B12 coenzyme, cobalt-carbon bond, factors affecting, 531 Bond leng hs:

aquocyanocobyric acid, 206 cobaloximes, axial phosphincs, 83 cobalt-carbon bond, steric crowding, 505 corrin, table, 48, 49 15-cyano-l,2,2,7,7,12,12-heptamethyl-

corrin, 206 isopropyl(pyridinc) cobaloxime, cobalt-

carbon bond,505 isopropyl(tricyclohexylphosphine)-

cobaloximc, cobalt-carbon bond, 506

isopropyl(triphenylphosphine)- cobaloxime, cobalt-carbon bond, 505

methyl(aquo)cobaloxime, cobalt-carbon bond,505

methyl(pyridine)bis(acetylacetone)- ethylenediiminecobalt,cobalt- carbon bond,505

methyl(pyridine)cobaloxime,obalt- carbon bond, 505

13C, biosynthetic studies: dicyanocobalamin, nmr spectrum, 112 vitamin B12, nmr spectrum, 112, 480

C-12, first step in corrin biosynthesis, decarboxylation, 120

C-13 epimer, neovitamin B12, 33 C-Iactone structure, vitamin B12, 227 C. tetanomorphum:

Factor I, isolation from, 130 nucleoside triphosphates, adenosylation, 160 sirohydrochlorin, incorporation into,

123 Cadmium:

alkylation, trans-dimethylcobalt(III) complexes, 527 incorporation into 15-cyano-l,2,2,7,7,12, 12-heptame hylcorrin, 211 Calcula ions, vitamin B12 coenzyme, electronic spectrum, 398 (+)Camphor: conversion to c/s-isoketipinic acid, 174 ring C, vitamin B12 total synthesis, 184 vitamin B12 total synthesis, 174, 193 Camphorquinone: vitamin B12 total synthesis, 183 Canonical resonance structures: corrin, 205 vitamin B12, 205 Capped cobaloximes: model systems, vitamin B12 coenzyme,

533,565 structure, 269, 533, 565 Carbanion intermediates, methylmalonyl- CoA mutase, 556 Carbanions: bis(salicylaldehyde)ethylenediiminecobalt(III), reaction with, 279 cobalt(III) complexes, reaction with, 279 Carbenes, reaction with cobalt(III)

complexes, 279 p-Carbomethoxyphenylcobinamide,

preparation, 271 Carbon dioxide, reduction to, acetic acid,

methylcobalamin, 528 Carbonium ion mechanism, isomerase

reactions, 377 Carbon monoxide: cobalt-carbon bond, reductive

cleavage, 515 oxidation, cobalt(III) complexes,

515

Carbon-skeleton rearrangements: epr spectroscopy, 381 mechanism, 385 protein-free models, 377 rearrangements, role of cobalt-carbon ntermediate, 382 Carbonylcobaloxime, 309 Carboxylatopentaaminecobalt(III) omplexes, photolysis, 272 Carboxylic acids: corrin oxidation, 218 preparation, vitamin B12, 231 Carboxymethylcellulose, corrin chromatography, 249 Carboxymethylcobalamin: borohydride cleavage, 303 lanthanide shift reagents, nmr spectrum, 472

photolysis, 302 pKa values, 316

spin-lattice relaxation imes, 492 Carboxymethylcobaloxime, thermolysis, 304 Carboxymethylcyanocobalamin, electronic spectrum, 413 15-Carboxy-15-norcobinamide: decarboxylation, 239 preparation, 239 vitamin B12, conversion to, 239 Catalysis, sodium borohydride reduction,

cobalt complexes, 252 Catalytic reduction, nickel 1,19-dimethyl-

octadehydrocorrin, 238 Cation exchange resin, hydrolysis, alkyl- (pyridine)cobaloximes, 249 Cation radicals: alkylcobaloximes, 515,517 epr spectrum, alkylcobaloximes, 517 Cba, see Cobamides Cbi, see Cobinamides Cbl, see Cobalamins Cby, see Cobyric acid CD, see Circular dichroism Cell dimensions, corrin derivatives, 92-97 Cell free enzymes, corrin biosynthesis, 116 Cerium(III) hydroxide, cobinamide from

vitamin B12, 236 Charge-transfer:

cobaloximes, electronic spectrum, 419 corrin, 403 electronic spectrum, cobalt-carbon bond,

394,403

Chemical degradation, vitamin B12, 111 Chemical formulae, corrin derivatives,

92-97 Chemical shifts (nmr):

vitamin B12 coenzyme, 465, 470 vitamin B12/, 485 vitamin B12,485

Chemical synthesis: cobinamides, 152 vitamin B12, 172-197

Chirality: corrin, 209 vitamin B12, 170

Chiral methyl, methionine, 115 Chiroptic effects, corrin, 207 Chloramine T reaction with:

corrin, 215 vitamin B12, 215

Chlorination: dehydrovitamin B12, 215 electronic spectrum, vitamin B12, 215

vitamin B12, 215 l-Chloro-2,2-^/s(/?-chlorophenyl)ethylcobalamin: trans-4,4 -dichloros ilbene, decomposition, 304 Chlorocobalamin, 411 10-Chlorodehydrovitamin B12:

electronic spectrum, 215 preparation, 215 Chloromethylcobalamin, photolysis, 303 Chloromethylcobaloxime, thermolysis, 304 Chlorosulfonyl isocyanate, cyanation of

corrin, 213 Chromatography: acid hydrolysis products, vitamin B12,

230 alkylcobaloximes, 247 carboxymethylcellulose, corrin, 249 cobaloximes, 247 corrin, ion exchange, 247, 249 DEAE cellulose, corrin, 249 neocorrinoids, 222 phosphocellulose, corrin, 249 separation of neo and normal corrins, 222 sephadex, corrin , 249

Chromic acid oxidation: dehydrocobinamide, 226

vitamin B12, 218 Chromium(II), cobalt complexes, reduction, 254

CIDNP measurements, radical pair recombination, 512 Cinnamyl(imidazole)cobaloxime, reaction with tetracyanoethylene, 286 Circular dichroism: aquocobalamin, 420 binding of corrin to apoenzyme, 423 cobalt-free corrin, 421 cobinamides, 421 cobyric acid, 421 corrin: pentadecaalkyl from, 237 sign inversion, 420-426 dicyanocobinamide, 421, 424 a, b-isomers, corrin, 421 methylcobalamin, 420 neocorrinoids, 8-epicorrinoids, 222, 225 protein bound, 426 sirohydrochlorin, 122 tetracarboxylic acid, 421 vitaminB12, 223,420 vitaminB12 coenzyme, 421 cis-Effect: cobaloximes, 85 corrin, 330 nmr spectroscopy: cobalt complexes, 487 corrin, 487 vitamin B12 halogenation, 216 cis-Isoketipinic acid, (+)camphor conversion to,174 Claisen rearrangement, amidoacetal, vitamin B12 total synthesis, 184 Cleavage: cobalt-carbon bond: photolytic, 524

vitamin B12 coenzyme, 547-554 electrophilic, cobalt-carbon bond, 526 energetics, cobalt-carbon bond, 551 halogens, cobalt-carbon bond, 516, 526 homolytic, cobalt-carbon bond, 524 induc ion, vitamin B12 coenzyme, cobalt- carbon bond,550 mercury(II), cobalt-carbon bond, 526 methylcobalamin, iodine, 316 models, cobalt-carbon bond, 88 modified cobalamins, cobalt-carbon bond, 65 nucleophilic attack, cobalt-carbon bond,

527

trifluoromethylcobaloxime, reaction wi h hydroxide, 309 Cob(I)inamide:

electronic spectrum, 419 nucleophilicity, 250, 251 see also Vitamin B128

Cob(II)alamin, see Vitamin B121. methyl radicals, recombination, 511

Cob(II) aloximes: alkylation, axial ligand effects, 519 dispropor ionation, 253 photolysis, methylcobaloxime, 301 reaction with:

equilibrium data, 504 kinetics, 504

1-phenylethylcobaloximes, 504 Cob(II)amides: epr spectrum simulation, table, 446 fifth axial ligands, epr parameters, table, 444 Cob(II)inamides:

electronic spectrum, 418 epr spectroscopy: angular anomalies, 443 anisotropic hyperfine interaction, 443

function of fifth ligand, table, 444 epr spectrum, high pH, 434, table, 447 magnetic circular dichroism, 426 oxygenation, epr spectrum, 458 Cobalamin auxotrophs, 163 Cobalamin coenzymes, interconversion, 163 Cobalamin phosphate, dephosphorylation,

E. coli alkaline phosphatase, 155 Cobalamin reductases, 158 Cobalamins: aggregation, 491

alkylcorrins vs. cobinamides, 369 biosynthesis:

addition of lower base, 153 Aerobacter aerogenes, 160 Clostridium sticklandii, 153 from cobyric acid, 148 L. Ieichmannii, 160 nicotinate mononucleotides, 153 5-phosphoribosyl-l-pyrophosphate,

153 ribose-l-phosphate, 153

bound to human intrinsic factor, table, electronic spectrum, 417

cobyric acid, conversion to, 148 configurations, N-glycosides, 153

Cleavage (Cont'd) radical transfer, cobalt-carbon bond, 526 stereochemistry, (S)-methylheptyl-

pyridinatocobaloxime, iodine, 317

thallium(III), cobalt-carbon bond, 526 vitamin B12 coenzyme, iodine, 316

Clostridium sticklandii, cobalamins, biosynthesis, 153

Clostridium teta nomorphum, source o f corrin, 146

Clostridium thermoaceticum, methylcobalamin biosynthesis, 161

CMS, see Vitamin B12 carboxylic acids Coa-aquo-Cob-adenosyl(3,5,6-trimethyl-

benzimidazolecobamide), reaction with cyanide, 306

Coa-cyano-Co/3-alkylcobamides preparation, 307

Coa-[a-(5,6-dimethylbenzimidazolyl] - Co/3-adenosylcobamide, see Vitamin B12 coenzyme

Coa-[ a-(5,6-dimethylbenzimidazolyl ]- Cob-(5-deoxy-5-adenosyl)cobamide, see Vitamin B12 coenzyme

Co(BAE), see bis{Acetylacetone)ethylenediiminecobalt; Cobalt complexes

Co(cHx2H2),see bis(l,2-Cyclohexane- dionedioximato) cobalt; Cobalt complexes

Co(cP2H2),see bis(l,2-Cyclopentane- dioximato) cobalt; Cobalt complexes

Co(D2B2F4),see Cobaloxime-BF2 bridged; Cobalt complexes

Co(D2H2),see Cobaloxime; Cobalt complexes

Co(SALEN), see Ms(Salicylaldehyde)- e hylenediiminecobalt; Cobalt complexes Co(SALOPH), see bis(Salicylaldehyde-o- phenylenediiminecobalt; Cobalt complexes Cob(I)alamin, see Vitamin B128

Cob(I)aloxime: alkylation: alkyl halides, 523 olefin addi ion, 523 stereochemistry, 523 l,l-Ms-(p-chlorophenyl)-2,2,2-trichloro-

ethane, reaction with, 266 2-hydroxyethylcobaloxime, reaction

with alkali, 310 nucleophilicity, 523

Cobalamins (Cont'd) conversion to vitamin B12 coenzyme,

156 coordination, mercury(II), 495 correlation between nmr and electronic

spectrum, 418 deficiency, 157 as-diaminoplatinum(II) coordination,

495 electron (hydrated), 254

FAD, 157 FMN, 157 NADH, 157

epr comparison to cobinamides, 448 epr spectroscopy, 433-442 isomeric forms, nmr spectroscopy, 484 13C-Iabelled, 474 nmr spectroscopy:

fluxionality, 490 pH dependence, 493

temperature dependence, 463-500 nmr spectrum, 474 nomenclature, 17 nucleotide loop biosynthesis, 148 prototrophs, 155 reaction with metal ions, 495 secondary alkyl, 255 zinc, 253 Cobalocorrin, structure, 203 Cobaloxime, structure, 246 Cobaloxime-BF2 bridged, nucleophilicity

cobalt(I), 251 Cobaloxime, structure, 246 Cobaloximes: addition to olefins, mechanism, 264 alkylation:

hydrazines and oxygen, 275 kinetics, table, 259

aryl derivatives, 270 axial phosphines, bond lengths, 83 bridged dimers, 268 chromatography, 247 m-effect, 85 cobalt ligand bond distances, tables,

82-84 dimethylsulfide complexes, 248 electronic spectrum, charge-transfer,

419 folding, 59 hydrogen reduction, 252 intramolecularly bridged, 269 MO-calculations, 419 model for corrin, 419

nmr spectrum, 247 nucleophilicity, cobalt(I) complexes, 251 optically active, alkyl ligands, 268 photolysis, 419 planarity deviations, 505 reduction, sodium borohydride, 251 reductive alkylation, 248 steric effects, 86 structure, 246 ter iary alkyl, 254 fraws-effect, table, 82 X-ray crystallographic data, 80-90 X-ray crystallography, vitamin B12, 23-106

Cobalt: alkylation, nitromethane, 280 cobalt complexes, electronegativity, 490 coordination, 47 hydrides:

pK values, 335 stability, 335, 365

incorporation into: 15-cyano-l,2,2,7,7,12,12-heptamethyl-

corrin, 211 vitamin B12, 211 model systems, 378 organic radical rearrangements, role of, 533 recombination with alkyl radicals, 335 reduced, X-ray crystallography, 69 reduction by alkali, B128 formation, 226 role in vitamin B12 chemistry, 333, 335 unique biologically, redox chemistry, 340

Cobalt 15-cyano-2,2,7,7,12,12-hexamethylcorrin: electronic spectrum, 424 structure, 423

Cobalt 15-cyano-7,7,12,12,19-pentamethylcorrin:

electronic spectrum, 424 magnetic circular dichroism, 424

Cobalt 15-cy ano-7,7,12,12-tetramethylcorrin: electronic spectrum, 424 structure, 423

Cobalt 2,2,7,7,12,12,15-heptamethylcorrin electronic spectrum, 424 structure, 423

Cobalt 2,2,7,7,12,12-hexamethylcorrin: electronic spectrum, 424 structure, 423

model systems, vitamin B12 coenzyme, 551

modified cobalamins, 65 nucleophilic attack, 527 radical transfer, 526 thalium(III),526

vitamin B12 coenzyme, acid 312, enzymic reactions, 507, 547 covalent, comparison to C-C bond, 337 covalent bond, 335 dissociation energy determination:

equilibrium, 507 kinetics, 511 photochemical, 507 thermochemical, 507

distortion,protein, 373 energies, 554 energy, 1,4,8,11 -tetraazacy clotetra-

decanecobalt(III), 554 factors affecting bond dissociation energy,

VitaminB12 coenzyme, 531 formation:

alkylation, cobalt(III) complexes, 517 CoOEP, 279

halogen cleavage, stereochemistry, 317 heterolytic cleavage, 305-319 homolysis, enzymic reaction, 456 homolytic cleavage, 296, 362 I nsertion of dioxgen, 512 l abilization, protein, 333 labilization by steric interactions, 361 l ength, alkylcobalt complexes, table,

505 lengths, 54

alkylcobaloximes, 359 I sopropylcobaloxime, 359 metalloporphyrins, 246 models for cleavage, vitamin B12 coenzyme, 551 photochemical cleavage, 362, 524 photolysis, 296 polarizability, nmr spectroscopy, 489 preparation, cobalt(III) complexes, 271-277 protection by peripheral groups, 90 protection by side chains, vitamin B12

coenzyme, 41 pyrolysis, 303 reaction with electrophiles, 312-317 reductive cleavage:

carbon monoxide, 515 thiols, 317,515

role of 4s and 4p orbitals, 338

Cobalt 7,7,12,12-tetramethylcorrin: electronic spectrum, 424 structure, 423 Cobalt carbenes, 576 Cobalt-carbon bond: activation enthalpy: homolytic cleavage, 511 kinetics, 511 biosyn hesis: eukaryotes, 155 prokaryotes, 155 timing, 155 bond angles: b-elimination, 369 protein effects, 373 steric effects, 355, 372 bond dissociation energy: axial ligands, 531 conforma ional changes, 531 1-cyanoethylcobaloxime, 511 isopropylcobaloxime, 511 1-methyl-heptylcobaloxime, 507, 511 l-methyl-2-phenylethylcobaloxime, 511 steric effects, 531 bond lengths: isopropyl(pyridine)cobaloxime, 505 isopropyl(tricyclohexylphosphine)-

cobaloxime, 506 isopropyl(triphenylphosphine)-

cobaloxime, 505 methyl(aquo)cobaloxime, 505 methyl(pyridine)£/s(acetylacetone)- ethylenediiminecobalt, 505 methyl(pyridine)cobaloxime, 505 methyl(triphenylphosphine)cobaloxime, 505 vinyl(pyridine)Z>/s(salicylaldehyde)-

ethylenediiminecobalt, 505 vinyl(pyridine)cobaloxime, 505

vitamin B12 coenzyme, 505 bond strength, vitamin B12 coenzyme, 513 charge-transfer, electronic spectrum, 404 cleavage:

corrin ring, distortion, 65 cyanide, 306 electrophilic, 526 energetics, 551 halogens, 516, 526 homolytic, 524 induction, vitamin B12 coenzyme, 550 mercury(II), 526 models, 88

sodium reduction, 254 trans-effect, nmr spectroscopy, 488 see also Alkylcobalt complexes Cobalt corrin: bond angles, tables, 45-53 bond distances, tables, 45-53 folding, 60 planarity deviations, 61 torsion around A-D junction, 57 Cobalt-free corrin: circular dichroism, 421 electronic spectrum, pH, 401 fluorescence spectrum, 402, 422 from Bacterium chromatium, 401 magnetic circular dichroism, 423 Cobalt-free corrinoid: electronic spectrum, 413 luminescence, 426 Cobalt orbitals, interaction with corrin

7r-orbitals, 561 Cobalt porphyrins, alkylation, diazo-

alkanes, 281 Cobalt role, vitamin B12 coenzyme enzymic

reaction, 555 Cobalt(I) complexes: acetylene, addition to, 256 acrylonitrile: addition to, 256 olefin IT -complexes, 527 addition to: olefins, mechanism, 265 unsaturated electrophiles, 256 a lkylation: alkyl halides, 523 electron transfer, 259 kinetics, 258 olefin addition, 523 tereochemistry, 502, 523 alkylcobalt(III) complexes, trans-

alkylation, 527 alkynes, addition to, 256 Cobaloxime-BF2 bridged, nucleophilicity, 251 cobaloximes, nucleophilicity, 251 bis(l,2-cyclopentanedioximato) cobalt,

nucleophilicity, 251 decomposition, 252 diacetylmonoximeimino diacetylmono-

ximatoiminopropane-1,3-cobalt, nucleophilicity, 251

threo-3,3-dimethylbuty 1-1,2,2- trifluoromethyl sulfonate, reaction wi h, 260

Cobalt-carbon bond (Cont'd) stability, 330, 335 stability vs. metal, 339 steric compression, distortion, 359 steric crowding, bond length, 505, 506 steric effects, bond dissociation energy,

512 synthesis:

analysis of reaction mixtures, 247 work up of reaction mixtures, 248

thermal cleavage, 362 thermal dissociation, 1-phenylethyl-

(pyridine)cobaloxime, 509 thermodynamic stability, 336 thermolysis:

alkylcobalamins, 525 alkylcobalt complexes, 525

VitaminB12 coenzyme: acid decomposition, 366 alkaline decomposition, 366 cleavage, 547-554 5 '-deadenosyl carbanion, and elimina-

tion, 549 5 '-deadenosyl carbocation, 548 5 '-deadenosyl radical, 548 heterolytic cleavage, 548 homolytic cleavage, 548

stability, 366 vitamin B12s, photolysis, 297 Cobalt-carbon intermediates, vitamin B12

coenzyme, 382 Cobalt complexes: alkylating agents, 254 alkylation, hydrazines and oxygen, 275 catalysis, sodium borohydride, 252 cis-effect, nmr spectroscopy, 487 electronegativity, cobalt, 490 hydrogen, reduction, 252 mechanism, reductive alkylation, 258-267 potassium, reduction, 254 redox chemistry, Schiff-base complexes,

514 reduction:

chromium(II), 254 electrochemistry, 254 sodium borohydride, 251 thiols, 254

reductive alkylation, 250 reductive arylation, electron transfer

mechanism, 271 rhodium corrin, comparison to, 72 sodium amalgam reduction, 254 sodium borohydride reduction, 251

Cobalt(I) complexes (Cont'd) effect of axial ligands, nucleophilicity,

252 electron-donor strength, ligand redox

potential, 504 electronic spectrum, 262 epoxides, reaction with, 256 equilibrium, hydridocobalt complexes,

506 etheneimine, reaction with, 257 mechanism, olefin addition, 262 methylacrylate addition, 256 nmr spectroscopy, 486 nucleophilicity:

effect of axial ligands, 252 table, 251

olefins, addi ion, 256 phenylacetylene, addition, 256 pH function, olefins, 523 preferred coordination number, 504 propargyl alcohol, addition, 256 propyne addition, 256 reactions, 263 redox potential, table, 251 stereochemistry, vinyl halides, alkylation, 260 3,3,3-trifluoropropyne, addition, 257 see also Cob(I)inamide; Hydridocobala- min; Hydridocobaloxime; Vitamin

1 2 S

Cobalt(II) complexes: alkylation: alkyl halides, 518

alkyl iodides vs. other alkyl halides, 522

radical intermediates, 518 electronic structure, 438 epr spectroscopy, 433 halogen abstraction, alkyl halides, 274, 519 methyl radicals, recombination with,

335 nmr spectroscopy, 486 orbitals, 438, 440 organic radical interaction, epr spectrum,

450 outer-sphere electron transfer, Schiff-base

complexes, 519 preferred coordination number, 504 reaction with:

alkyl halides, 273 kinetics, 273, 274, table organic radicals, 271

reactivity toward alkyl halides, table, 521

spin-Hamiltonian, 436 Cobalt(III) complexes: acetylene, carbanion reaction, 279 alkylation:

acetone, 517 diazoalkanes, 281 Grignard reagent, 277, 517 organolithium reagents, 517

carbenes, reaction with, 279 carbon monoxide, oxidation, 515 cobalt-carbon bond:

formation, alkylation, 517-524 preparation, 271-277 electronic spectrum, 394 enols, reaction with, 279 ethyl vinyl ether, reaction with, 281 2-hydroxyethylvinyl ether, reaction with, 282

malononitrile, reaction with, 279 nucleophilic attack, 284 olefin 7r-complexes, 282 photoaquation, 296 photoreduction, 296 preferred, coordination number, 504 reaction with: carbanions, 279 vinyl e hers, 281 stable, five coordinate, 506 zwitterionic, 286 Cobalt(IY) complexes, 514 Cobalt(II) substrate radical separation, vitamin B12 coenzyme enzymic reaction, 452 Cobamic acid, nomenclature, 17 Cobester, see Heptamethylcobyrinic acid Cobinamide guanosine diphosphate, 5,6-dimethylbenzimidazole-5 - nucleotide, reaction with, 153 Cobinamide phosphate, addition of guanosine diphosphate, 152 Cobinamides: biosynthesis, 151, 152 chemical synthesis, 152 circular dichrosim, 421 vs. cobalamins, alkylcorrins, 369 electronic spectrum, 415 enzymic preparation, 152 epr spectroscopy, 442-448 equilibria, 5- and 6-coordinate, table, 350

formation, 234

Cobinamides (Cont'd) a, b -isomers, electronic spectrum, 413

table, 416 steric interactions, epr spectrum, 448 structure, 235 from vitamin B12, cerium(III) hydroxide,

236 vitamin B12 , conversion to, 234

Cobinic acid, nomenclature, 17 Cobyric acid:

bond angles, tables, 45-53 bond distances, tables, 45-53 cell dimensions, 94 chemical formula, 94 circular dichroism, 421 cobyric acid a and b , 197 conversion to cobalamins, 148

VitaminB12, 197 electronic spectrum, 415 folding, 60 formation, 235 planarity deviations, 61 space group, 94 structure, 34, 148, 170 torsion around A-D junc ion,

57 total synthesis, 187, 196 trimethylated isobacteriochlorins,

incorporation into, 132 vitamin B12 , conversion to, 235 X-ray crystallographic data, 94 X-ray diffraction data, diagram, 34 Cobyric acid a and b, 197 Cobyrinic acid, acid hydrolysis, vitamin B12, 230 biosynthesis: origin of carbon atoms, 112 primary precursors, 111 uroporphyrinogen(III) as precursor, 116 Factor I: incorporation into, 131 reduced form, incorporation into, 131

nomenclature, 17 sirohydrochlorin, incorporation into,

123 structure, 109

uroporphyrinogen III, biosynthetic precursor, 116 Cobyrinic acid a,c-diamide: preparation, 37

X-ray crystal structure (diagram), 34

Co [(CO)(DOH)pn], see Diacetylmono ximeimino diacetylmonoximatoiminopropane-l,3-cobalt; Cobalt complexes Coenzyme, see Vitamin B12 coenzyme Coenzyme B12 , see Vitamin B12 coenzyme Coenzyme func ion, vitamin B12 s, 147 Cofa ctor:

2,6-diaminohexanoate mutase, pyridoxal phosphate, 574

glutathione, nucleotide loop biosynthesis. 152

Color and clinical activity, vitamin B12, 8 Comparison to: cobalt complexes, rhodium corrin, 72 crystal structure, conformations, 482 model systems: vitamin B12,504 vitamin B12 coenzyme, 504 vitamin B12, nonvitamin B12, 35 vitamin B12 coenzyme, table, vitamin B12, 53 X-ray structure, nmr spectroscopy, molecular structure in solution, 482 Configurational interactions, electronic

spectrum, 398, 404 Configurations: corrin, 209

N-glycosides, cobalamins, 153 Conformational changes:

cobalt-carbon bond, bond dissociation energy, 531 vitamin B12 coenzyme, 374 Conformations: alkylcobalamins, 341 comparison to crystal structure, 482 corrin, table, 50, 51 corrin ring side chain, 52, 54, 63 corrin side chain, 207, 341 electronic structure and spectrum, 343 neovitamin B12, 209 nickel( II) 15 -cy ano-7,7,12,12,19- pentamethylcorrin chloride, 208

nucleosides, 70 nucleotide loop, 65 nucleotides, 70 side chain, 52, 54 vitamin B12 :

ribose ring, 550, 554 side chain, 208

Conjugated system: addition to corrin, 238

Copper analog, vitamin B12 , 211 Copper cobalamin, magnetic circular dich-

roism, 426 Copper incorporation into vitamin B12,

211 Correlation between nmr and electronic spectrum, cobalamins, 418 Corrin biosynthesis: bilanes: aminomethyl, 117 hydroxy methyl, 118 1-methyl, 121 broken cell enzymes, 116 cell free enzymes, 116 decarboxylation, C-12, first step, 120 porphobilinogen deaminase, 117 secocorrins, intermediates in, 116 spirocyclic intermediate, 118 uroporphyrinogen III, loss of, C-20, 137, 139, 145-167 Corrin p-orbitals, cobalt orbitals, interactions, 561 Corrin precursor, aminomethylbilane, 117 Corrin reduction, ferredoxin, 254 Corrin ring:

S-adenosylmethionine, activation, 345 C-10 chemical shifts vs. electronic

spectrum, 487 conjugation, 61 deforma ions, 63 5 '-deoxyadenosyl ligand, interactions

with, 66 5,6-dimethylbenzimidazole, interaction

with, 28,353 distortion, cobalt-carbon bond cleavage,

65 folding, benzimidazole effect on, 59,

60 (table) gadolinium(III), shift reagent, 472,

482 nmr spectrum: C-10 proton, 469

lanthanide shift reagents, 471, 482 paramagnetic shifts, 471 1H/2 H exchange, 469 nmr spectrum(13C), 479

side chain, 480 planarity, 54 puckering, 54 side chain, conformations, 52, 54, 63 vitamin B12 coenzyme, nmr spectrum, 469

Conjugated system (Cont'd) corrin, 61, 203 vitamin B12, 238 Constraint of axial ligands, vitamin B12

conezyme, 41 Conversion to: 2-alkoxyalkylcobaloximes, 2-acetoxy-

alkylcobaloximes, 575 D-l-amino-2-propanol, L- hreonine, 199 15-carboxy-l5-norcobinamide, vitamin

B12, 239 cobalamins, cobyric acid, 148 cobinamides, vitamin B12, 234 cobyric acid, vitamin B12 , 235 dicyanocobalamin, standard electronic

spectrum for vitamin B12, 395 heptamethyl dicyano-5, 15-bisnorcobyrinate, vitamin B12, 239 heptamethyl dicyanocobyrinate, vitamin B12, 236 c/s-isoketipinic acid, (+)camphor, 174 methylcobalamin, vitamin B12 coenzyme, 163

sirolactone, sirohydrochlorin, 123 vitamin B12, cobyric acid, 197 vitamin B12 coenzyme, cobalamins, 156 methylcobalamin, 163 CoOEP, cobalt-carbon bond formation, 279 5- and 6-Coordinate:

alkylcobalamins, 346, 351 cobinamides, equilibria, 350 corrin, axial ligands, 346 homolytic cleavage, 371 vitamin B12 coenzyme, 346

Coordination: alkylcobalamins, cw-diaminoplatinum(II),

495 alkylcorrins, imidazole, 358 cobalamins, cw-diaminoplatinum(II), 495 cobalt, 47 mercury(II), cobalamins, 495 l-(2-trifluoromethylphenyl)imidazole,

heptamethylcobyrinate, 495 vitamin B12 coenzyme, c/s-diamino-

platinum(II), 497 vitamin B128, 5,6-dimethylbenzimidazole,

486 Coordination chemistry:

adenylcobamide, 351 vitamin B12, 325-392 Coordination number, cobalt complexes, 504

Corrin: adenosylation, 155 affinity chromatography, 268 alkylation, 214 alkyl ligands, effect on physical properties,

table, 356 5-aminolevulinic acid, incorporation into,

111 aromaticity, 204 axial ligands:

5- and 6-coordinate, 346 steric requirements, 255

bioxynthesis: Euglena gracilis, 117 1-methylbilane, 107-144 Propionibacterium shermanii , 112

bond angles, di stances, table s, 45-53 bond lengths, observed and calculated, 205,48 table, 49, 206 bromination, 215 buckling, 208, 342 canonical resonance structures, 205 charge-transfer, 403 chirality, 209 chiroptic effects, 207 chloramine T, reac ion with, 215 chlorosulfonyl isocyanate, cyanation, 213 chromatography:

carboxymethylcellulose, 249 DEAE cellulose, 249 phosphocellulose, 249 separation of neo and normal, 222

Sephadex, 247, 249 circular dichroism,a, 0-isomers, 420-426 cis-effect, nmr spectroscopy, 330, 487 Clostridium tetanomorphum, source of, 146 configurations, 209 conformations, 50, 51, 207, 341 conjugated system, addition to, 203, 238 5-coordinate, decomposition, alkyl

cobalamins, 369 crystallization, 249 cyanation, 213 cyclization (peripheral):

lactam formation, 225 lactone formation, 226 xanthocorrinoids, 228

dehydrogenation, 238 demetallation, 210 deuteration, 212, 220 dimethylaminomethylation, 213

dimethyl(methylene)ammonium iodide, reaction with, 213

distortion, 207 electronic spectrum, polarization effects,

393-430 electrophilic substitution, MO-calcula ions, 212,345 electrophoresis, 249 epimerization, equilibrium constants, table, 222

mechanism, 224 MO-calculations, 220 trifluoroacetic acid, 222

epimers, 210 folding, 60 halogenation, 204, 215 helicity, 209 hydrated electrons, reaction with, 318 Ion exchange chromatography, 249 13C-Iabelled, 474 lack of aromaticity, 204 lactam formation, 225 lactone formation, 226 laser Raman spectrum, 343 ligand substitution roles, 330 ligand substitutions, 337 luminescence, 426 cobalt-free, 426 macrocycle reactions, 201-243 magic Mannich, dimethylaminome hyla tion, 213 magnetic properties, 330 meso-methyl groups:

oxidation, 239 pKa values, 239

meso-substitution, 212 metal-free, electronic spectrum, 207 metallation, 210-212 methionine:

incorporation into, 111 CD3-methyl, incorporation into, 114

p -molecular orbitals, 397 nitrosation, 217 nitrosyl chloride, reaction with, 217 nmr spectroscopy, 463-500 nomenclature, 18 nucleotide loop biosyn hesis, 148 orbital energies, 206, 399 organic solvent soluble, prepara ion, 236 organocobalt complexes, (review), 330 oxidation:

carboxylic acids, 218 chromic acid, 218

Corrin (Cont'd) hydrogen peroxide, 218

oxidative cleavage, succinimides, 217-220 ozonolysis, secocorrindione, 218, 219 paper chromatography, 249 permanganate oxidation, 218, 219 pentadecaalky! from vitamin B12, 236 circular dichroism, 237 phenol extraction, 249 phenylthiomethyl chloride, reaction with, 214 photoaquation, 330 planarity, deviations, 61, 208 porphobilinogen, incorporation into, 111 Propionibacterium shermanii, source of, 146 radical recombination, 363 resonance Raman spectrum, 398 secocorrindione cyclization, 219 side chain conformations, 63, 208 sign inversion, circular dichroism, 422 steric effects:

origin, 355 transmission, 355 strain orbital, 400, 411 torsion around A-D junction, 57 trans-effect, nmr spectroscopy, 80, 330, 487 uroporphyrinogen III, intact incorporation into, 117 varia ion with temperature, electronic

spectrum, 348 see also Cobalamin; Metallocorrins; Specific metallocorrins; Yellow corrinoids Corriphyrin-3: isolation, 134 nmr spectrum, 135 structure, 134 Corriphyrin-4, structure, 124, 128 Corriphyrins, 121. Seealso

Sirohydrochlorin Corrole:

bond angles, distances, tables, 45-53 folding, 60 nomenclature, 19 structure, 203 torsion around A-D junction, 57

Cosynthetase, see Uroporphyrinogen III cosynthetase

CoTPP, disproportionation: alkylation, 279 in basic DMSO, 279

Coupling east and west halves, vitamin B12

total synthesis, 169-200 Covalent bond, cobalt-carbon bond, 335 CrystalUzation:

alkylcobaloximes, 248 corrin, 249

Crystal morphology: pleochroism vitamin B12, 26 refractive index, vitamin B12, 26

Crystal structure, conformations, comparison to, 482

Cyanation: corrin, chlorosulfonyl isocyanate, 213 vitamin B12, 213

Cyanatocobalamin, electronic spectrum, 411

Cyanide: acetonitrile formation, methylcobaloxime,

307 L-adenosylcobalamin, reaction with, 306 ara-adenosylcobalamin, reaction with, 306 alkylcobalamins, reaction with, 306 aristeromycyclocobalamin, reaction with, 306 N-benzoyladenosylcobalamin, reaction

with, 306 Coa-adenyl-Co/3-adenosylcobalamin,

reaction with, 305 Coa-aquo-Co/3-adenosylcobamide, reac-

tion with, 306 Coa-aquo-Co/3-adenosyl(3,5,6-trimethyl-

benzimidazolecobamide), reaction wi h, 306

cobalt-carbon bond cleavage, 306 difluorochloromethylcobalamin, reaction

with, 307 D-erythro-2,3-dihydroxy-4-pentenal,

vitamin B12 coenzyme, 305 formycyclobalamin, reaction with, 307 pyrazolopyrimidine nucleosidylcobalamin,

reaction with, 307 N-tosylcytidylcobalamin, reaction with,

306 triethylaminoethylcobalamin, reaction

with, 307 trifluoromethylcobalamin, reaction

with, 307 vitamin B12 coenzyme, reac ion with, 305 15-Cyano-l,2,2,7,7,12,12-heptamethylcorrin: bond lengths, 206 cadmium, incorpora ion into, 211 cobalt incorporation into, 211

15-Cyano-l,2,2,7,7,12,12-heptamethylcorrin (Cont'd) electronic spectrum, 401 lithium, incorporation into, 211 metallation, 211 nickel, incorporation into, 211 rhodium, incorporation into, 211 structure, 211

zinc, incorporation into, 211 15-Cyano-l, 2,2,7,7,12,12-heptamethylcorrin hydrochloride: cell dimensions, 95 chemical formula, 95 space group, 96 X-ray crystallographic data, 96 Cyano-1,8,8,13,13-pentamethyl-5-cyano- 16-ethoxy-14-[2-imino-propenyl] - CD secocorrin perchlorate: cell dimensions, 97 chemical formula, 97 space group, 97 X-ray diffraction data, 97 Cyanoaquocobinamide, a,b-isomers, nmr

spectrum, 484 Cyanobromide vitamin B12, total synthesis, 169-200 Cyanocobalamin: vitamin B12, 17 see also Vitamin B12

R-a -cyanoethyl(S-a -methylbenzylamine)- cobaloxime, racemization, X-ray crystallography, 88 Cyanoethylcobalamin: alkaline decomposition, 366 reaction with alkali, 310 1-Cyanoethylcobaloxime, cobalt-carbon bond, bond dissociation energy, 511 Cyanoimidazolecobinamide, electronic

spectrum, 343 Cyanomethylcobaloxime, thermolysis, 304 Cyclic nucleoside, structure, 554 Cyclic 2', 3', -ribazole phosphate,

vitamin B12 total synthesis, 194

8, 5'-Cyclic-adenosine, see 5'-Deoxy-8, 5'- cycloadenosine

Cyclization: corrin, secocorrindione, 219 5 '-deoxyadenosyl radical, 554 lactam formation, corrin, 225 lactone formation, corrin, 226 xanthocorrinoids, corrin, 228

Cyclobutylcobalamin, rate of decomposition, 368 Cyclodecyl-I-d-iodide, reaction with vitamin B128, 261 Cyclohexylcobalamin: electronic spectrum, 255 rate of decomposition, 368 CyclohexylcobaJoxime, thermolysis, 304 Cyclohexylnitrone, vitamin B12 total

synthesis, 192 Cyclohexyl-3, 5, 6-trimethylbenzimidazoyl-

cobamide, preparation, 255 Cyclopentylcobalamin, ra te o f decomposi-

tion, 368 Cyclopropane formation, pentacyanocobaltate

1,3-diiodopropane, 519 Cyclopropylcarbinylcobalamin r earrange-

ments, but-3 -enylcobalamin, 362, 379,567

Cyclopropylcarbinylcobaloxime rearrangements, 381

Cyclopropylcarbinyl(pyridine)cobaloxime rearrangements, but-3-enyl- (pyridine)cobaloxime, 568

Cyclopropylcarbinyl radical rearrangements, but-3-enyl radical kinetics, 557,567

Cyclopropylcobalamin, rate of decomposition, 368

Cyclopropyloxycorrinoid, 570 Cylindrical projection, X-ray structure, 97 Cysteinylcobalamin, ele ctronic spectrum,

411 Dansylamidopropylcobalamin pr eparation,

267 DBC, see Vitamin B12 coenzyme DEAE cellulose, corrin chromatography, 249 Dealkylation alkylcobalamins, thiols,

alkylcobaloximes, 527 Deamidation, nicotinate mononucleotides,

153 Deaminase, see Porphobilinogen deaminase Deamination: aminomethylbilanes, porphobilinogen deaminase, 117 bilanes, aminomethyl, 118 Decarboxylation: C-12, first step in corrin biosynthesis, 120

Decarboxylation (Cont'd) 15-carboxy-15-norcobinamide, 239 5,15-dicarboxy-5,15-dinorcobinamide, 239 [R] -l-amino-2-propanol, threonine,

150 Decomposition:

in acid, j3-hydroxyethylaquocobaloxime, 313 acid catalysis, alkylcorrins, 369 alkylcobalamins:

corrin five coordinate, 369 rate of, 365,368,370 very strained, rate of, 371

alkylcorrins, olefins, 365 1-chloro-2,2-Z>w(p-chlorophenyl)ethyl-

cobalamin, trans-4, 4'-dichlorostilbene, 304

cobalt(I) complexes, 252 cyclobutylcobalamin, rate, 368 cyclohexylcobalamin, rate, 368 cyclopentylcobalamin, rate, 368 cyclopropylcobalamin, rate, 368 methylcobalamin, rate, 368 neopentylcobalamin, rate, 368 2- norbornylcobalamin, rate, 368

Decyanation, vitamin B12, ferredoxin, 163

Deficiency, cobalamins, 157 Definition, nucleophilicity, 250 Deformations, corrin ring, 63 Dehalogenation, vitamin B12, 217 Dehydration:

1,2-dihydroxyethyl radical, 573 yellow corrinoids, 229

Dehydrocobinamide: chromic acid oxida ion, 226 mechanism of formation, 226 see also Lactams (corrin ring)

Dehydrocorrin: bond angles, distances, tables, 45-53 torsion around A-D junction, 57

Dehydrogenation, corrin, 238 Dehydrovitamin B12

chlorination, 215 structure, 215

Demetallation: corrin, 210 siroheme, 128 vitamin B12, 210

5 -Deoxyadenosine, 441, 558 hydrogen abstrac ion, 554 intermediate, vitamin B12 coenzyme, 332

VitaminB12 coenzyme: ribonucleotide reductase, 577 thiols, photolysis, 299, 545 [5'-3H]5'-deoxyadenosine, 298 5 '-Deoxyadenosyl carbanion, 549 5'- Deoxyadenosyl carbocation, stabiliza tion, 549 5 '-Deoxyadenosyl ligand: interactions with corrin ring, 66 nmr spectrum(13 C), 477 5 '-Deoxyadenosyl ligand, vitamin B12

coenzyme, nmr spectrum, 468 5 -2 H -Deoxyadenosyl ligand, nmr spectrum,

VitaminB12 coenzyme, 471 5'- Deoxyadenosyl radical: cyclization, 554 formation: 8-position modification, 298 reactions, 297, 363 reaction with vitamin B12r, 373 stabilization, 548 vitaminB12 coenzyme: enzymic reaction, 554 ribonucleotide reductase, 577 5 '-Deoxy-8,5 '-cycloadenosine: formation, 297 structure, 297 5'-Deoxy(l,N6 -etheno)-adenosylcobalamin, preparation, 285 5 '-Deoxy-5 '-halonucleoside preparation, vitamin B12 coenzyme analogs, 267 Dephosphorylation, cobalamin phosphate,

154 D -erythro -2,3-Dihydroxy-4 -pentenal, vitamin B12 coenzyme and cyanide, 305 Descobaltocobalamin, metallation, 211 Descobaltocobantide: electronic spectrum, pH, 211 metallation, 211 Descobaltocobyric acid, 211 Desulfoviridin, sirohydrochlorin isolation,

122 Deuteration: corrin, 212, 220

dicyanocobalt(III) tetramethylcorrin, 212

ethylcobinamide, 345 metallocorrins, 220 vitamin B12, hexacarboxylic acid, 212 see also 1 H/2 H exchange Deviations from planarity, corrins, 61

trans-4,4'-Dichlorostilbene, decomposition l-chloro-2,2- bis (p - chlorophenyl)- ethylcobalamin, 304

Dicobaloximes, preparation, 268

Dicyanocobalamin: electronic spectrum, 413 nmr spectrum, 13 C, biosynthetic

studies, 112 nmr spectrum, 13 CN enriched,

478 standard electronic spectrum,

vitamin B12, 395 table (13 C), nmr spectrum,

476 Dicyanocobalt(III) tetramethylcorrin,

deuteration, 212 Dicyanocobinamide:

circular dichroism, 421, 424 electronic spectrum, temperature

variation, 348, 395, 408, 424 table (13C), nmr spectrum, 476

Dicyanofcobyrinic acid-0,c-diamide]: cell dimensions, 94 chemical formula, 94 space group, 94 X-ray crystallographic data, 94

Dicyanocobyric acid, structure, 206 Dicyanocobyrinic acid, abcdeg hexamethyl

ester/-nitrile, 214 Dicyano-5,6- dihy droxy- dehydro-cobyrinic

acid pentamethylester-c,cMactone, see Yellow corrinoids

Dicy an o-5,6-dihy droxy-dehydro-cobyrinic hexamethy lester-c -lactone, see Yellow corroinoids

Dicyanoheptame hylcobyrinate, magnetic circular dichroism, 426

Dicyano-5-hydro-6-amino-dihy dr o-cobyrinic acid pentamethylester-fl-amide-c- lactam, see Yellow corrinoids

Dicyan o-5 -hydro - 6- amino - dihy dro- cobyrinic acid pentamethylester- OL-amide-c-lactam, see Yellow corrinoids

4', 5 -Didehydro-5 '-deoxyadenosine, 441

4', 5 '-Didehydro-5 '-deoxyaristeromycin: formation, 297

structure, 297, 308 Diels-Alder, Lewis-acid catalyzed, vitamin B12 total synthesis, 183

Diacetylmonoximeimino diacetylmonoximatoiminopropane-1,3- cobalt:

alkyl complexes, redox chemistry, 514 nucleophilicity, cobalt(I), 251, 523 pKa values, 504 redox potential, 504 structure, 503

Diacetylmonoximeimino diacetylmonoximatoiminopropane-1,3-cobalt(I):

alkyl complexes, photolysis, 524 nucleophilicity, 523

2,6-Diaminobularine, vitamin B12 coenzyme fluorescent analogs, 300

2,6-Diaminohexanoate mutase, pyridoxal phosphate co factor, 574

(R)-2,6-Diaminohexanoate, 546 (S)-3,6-Diaminohexanoate, 546 3.5- Diaminohexanoic acid, 328 2.5- Diaminonebutavinylcobalamin, preparation, 267 (R)-2,5-Diaminopentanoate, |3-leucine, 540,546 cis-Diaminoplatinum(II), coordination:

alkylcobalamins, 495 cobalamins, 495

vitaminB12 coenzyme, 497 2,4-Diaminovaleric acid, 328 Diaquocobinamide, formate reduction, 447 Diazene cobalt complexes, 275 Diazoalkanes:

cobalt(III) complexes, alkylation, 281

cobalt porphyrins, alkylation, 281 preparation, vinylcobalt porphyrins, 280

Diazomethane: esterification, basic conditions, vitamin

B12 total synthesis, 193 preparation of halomethylcobalt porphyrins, 280 Dibenzo-corromin, X-ray crystallographic data, 92 ab-Dibromoethyl acetate, vitamin B12

coenzyme reaction with, 285 5,15 -Dicarboxy-5,15 -dinorcobinamide: decarboxylation, 239 preparation, 239 5,6-Dichlorobenzimidazole, X-ray diffraction data, vitamin B12, 27 Dichloromethylcobalamin, photolysis, 303

2,2-Diethoxyethylcobalamin, preparation, 281

Diethylaminoethyl cellulose, see DEAE cellulose, corrin chromatography 8,12-Diethyl-2,3,7,13,17,18-hexamethyl- corrole: cell dimensions, 96 chemical formula, 96 hydrobromide, X-ray crystallographic

data, 96 space group, 96 X-ray crystallographic data, 96

Difference electron density map, X-ray structure, 97

Difluorochloromethylcobalamin, reaction with cyanide, 307

Dihalomethylcobaloximes, reaction with alkali, 309

Dihydromethylisobacteriochlorin, 141 Dihydrosirohydrochlorin, 139 Dihydroxyalkylcobaloximes, preparation,

284 Dihydroxyalkylcobalt complexes, models

for enzymic reaction, 572 1,2-Dihydroxyalkyl radicals, vitamin B12

coenzyme, diol dehydrase, 571 1,2-Dihydroxyethylcobalt, olefin 7r-com-

plexes, 574 2,2-Dihydroxy ethyl cobalt, olefin p

complexes, 574 1,2-Dihydroxyethyl radical: dehydration, 573 pulse radiolysis, 574 rearrangements, 532 4,5-Dihydroxy pentylcobaloxime: 1,2-dihydroxypentyl radical, 573 photolysis, pentanal, 534, 573 1.2- Dihydroxypentyl radical, 4,5-dihydroxy-

pentylcobaloxime, 573 Dihydroxypropylcobalamin: Dihydroxypropylcobalamin:

glyceraldehyde, photolysis, 302

glyceric acid, photolysis, 302 2.3- Dihydroxy-H-propylcobalamin:

periodate oxidation, 284

photolysis, 302 1,3-Diiodopropane, cyclopropane formation,

pentacyanocobaltate, 519 Dimeric complex with iodide, heptamethyl-

cob(II)yrinate, 522 Dimethylaminomethylation, corrin, magic Mannich, 213 vitamin B12, 213

Dimethylated isobacteriochlorins, structure, 123

Dimethyl(bromomethyl)malonate, reaction with vitamin B12 s , 564

Dimethyl(methylene)ammonium iodide, reaction with corrin, 213

5,6-Dimethylbenzimidazole: coordination, vitamin B128, 486 dissociation, 494 interaction with corrin ring, 353 nmr Spectrum(13C), 477 5 '-nucleoside, 154 pK values, 351

protonation, nmr spectroscopy, 494 steric interaction with corrin ring, epr

spectrum, 448 thermodynamics, Ugand exchange, table, 496 trans-cfted, nmr spectroscopy, 488 vitamin B12 coenzyme, nmr spectrum,

465,470 vitamin B12, total synthesis, 198 5,6-DimethylbenzimidazoIecob(II) inamide,

epr spectrum, 448 5,6-Dimethylbenzimidazole-5 '-nucleotide,

reaction with cobinamide guanosine diphosphate, 153

threo-3,3-Dimethylbutyl-l,2-tf 2 2-trifluoromethyl sulfonate, reaction with

cobalt(I) complexes, 260 fra^s-Dimethylcobalt(III) complexes,

heavy metal alkylation, 527 Dimethylmercury(II), methylcobalamin,

526 Dimethylsulfide complexes, cobaloximes,

248 Diol dehydrase:

1,2-dihydroxyalkyl radicals, vitamin B12

coenzyme, 571 enzymic reaction, bridged cation, 546, 555 epr spectroscopy, enzymic reaction, 558 inhibition, nitrous oxide, 373 MO-calculations, 557 model systems, vitamin B12 coenzyme,

532,571 radical intermediates, 556 reaction pathways, olefin ^-complexes,

555,558,575 vitamin B12 coenzyme, enzymic reaction,

529 1,2-Diols, radical rearrangements to alde-

hydes, 573

1,3-Dioxa-2-cyclopcntylmethylcobaloxime, preparation, 282

1,3-Dioxo-2-cyclopentylmethylcobalamin, reaction with acid, 315

Dioxygen, cobalt-carbon bond insertion,

512 Dipolar coupling, epr spectroscopy, 452 Direct methods, X-ray structure, 97 Disproportionation:

alkylation, CoTPP, 279 in basic DMSO, CoTPP, 279 cob(II)aloximes, 253 vitamin B12r ., 253 vitamin B12s, vitamin B121., 514

Dissociation energy: equilibrium, cobalt-carbon bond, 507 kinetics, cobalt-carbon bond, 511 photochemical, cobalt-carbon bond,

507 thermochemical, cobalt-carbon bond,

507 Dissociation-recombination pathway,

vitamin B12 coenzyme, enzymic reaction, 555

Distortion: cobalt-carbon bond, steric compression, 359,373 cobalt-carbon bond cleavage, corrin ring,

65 corrin, 207 vitamin B12 coenzyme, protein role, 372

DMBC, see Vitamin B12 coenzyme a-Donor power, ligands, 333

E. coli: alkaline phosphatase, cobalamin phosphate

dephosphorylation, 155 methylcobalamin, biosynthesis, 161 El/2, see Redox potential E2, see Vitamin B12, carboxylic acids, preparation; Vitamin B12, monocarboxylic acid Effect of axial ligands: alkyl ligands, pK values, 356 alkyl ligands, table, electronic spectrum, 356

7-band, electronic spectrum, 411 cobalt(I) complexes, nucleophilicity, 250,252

Effect on corrin ring folding, benzimidazole, 59

Effect on physical properties, corrin alkyl ligands, 356

Electrochemical oxidation: alkylcobaloximes, 515 methylcobalamin, 517 see also Redox chemistry; Redox potentiall Electrochemical reduction: cobalt complexes, 254 methylcobalamin, 318 methylcobinamide, 318 Electrocyclic ring opening, enzymic

reaction, vitamin B12 coenzyme, 576

Electron d ensity map, X -ray str ucture, 97

Electron ( hydrated), cobal amin r educ- tion, 254

Electron-donor strength, ligand redox potential, cobalt(I) complexes, 504

Electronegativity, cobalt complexes, 490 Electronic spectrum:

alkylcobaloximes, 406 aminocobalamin, 411 aquocobalamin, 417 aquocyanocobinamide, 408, 413 aquohydroxocobinamide, 413

axial ligands, 409, 412 azidocobalamin, 411, 417 calculations, vitamin B12 coenzyme,

398 carboxymethylcyanocobalamin, 413 charge-transfer, cobaloximes, 394, 403, 419 10-chlorodehydrovitamin B12, 215 cob(I)inamide, 419 cob(II)inamide, 418 cobalamins: bound to human intrinsic factor, table, 417

correlation between nmr and, 418 cobaloximes, 419 cobalt-carbon bond, charge-transfer,

404 cobalt 15 -cy ano-2,2,7,7,12,12-hexa-

methylcorrin, 424 cobalt 15 -cy ano-7,7,12,12,19-penta-

methylcorrin, 424 cobalt 15 -cyano-7,7,12,12-tetramethy 1-

corrin, 424 cobalt 2,2,7,7,12,12,15-heptamethyl-

corrin, 424 cobalt 2,2,7,7,12,12-hexamethylcorrin,

424

Electronic spectrum (Cont'd) cobalt 7,7,12,12-tetramethylcorrin, 424 cobalt(I) complexes, 262 cobalt(III) complexes, 394 cobalt-free corrinoid, 413 cobinamides, a, /3-isomers, 413, table, 415 cobyric acid, 415 configurational interactions, 398, 404 conformations, electronic structure, 343 corrin: metal-free, 207

variation with temperature, 348, 393- 430

corrin ring, C-IO chemical shifts, 487 cyanatocobalamin, 411 cyanoimidazolecobinamide, 343 15 -cyano-1,2,2,7,7,12,12-heptame thy 1-

corrin, 401 cyclohexylcobalamin, 255 cysteinylcobalamin, 411 dicyanocobalamin, 413 dicyanocobinamide, 395, 408, 424 effect, alkyl ligands table, 356 effect of axial ligands, table, 7-band,

411 enzyme-substrate complex, 375 ethylcobalamin, 408 ethylcobinamide, 408 ethylcyanocobalamin, 413 ethynylcobalamin, 411, 415 Factor I, 130 hydridocobalamin, 365 hydroxocobalamin, 404, 417 hydroxyethylcyanocobalamin, 413 imidazolecobalamin, 411 iodocobalamin, 411 isopropylcobalamin, 255, 408 isopropylcobinamide, 255, 408 LCAO-MO, 396 metal-free corrin, 395 metallocorrins, 424 me hylcobalamin, 408, 415 me hylcobinamide, 343, 408 methylcyanocobalamin, 413 me hylisocyanatocobalamin, 411 modification of corrin ring, 415 neocorrinoids, 222 nephelauxetic series, 409 nickel 15-cyano-7,7,12,12,19-pentamethyl-

corrin, 424 nickel 7,7,12,12,19-pentamethylcorrin,

424

10-nitrosocobalamin, 217 octamethyl ester, trimethylated isobacteriochlorins, 132 pH:

cobalt-free corrin, 401 descobaltocobamide, 211 phenolatocobalamin, 404 polarization effects, corrin, 402 n -propylcyanocobalamin, 413 pyridinatocobalamin, 411 selenocyanatocobalamin, 411 sirohydrochlorin, octamethyl ester, 123 solvent effects, 409 spin-forbidden transi ions, 406 sulfitocobalamin, 347, 411 sulfomethylcyanocobalamin, 413 temperature effects, 407 temperature variation:

alkylcobinamides, 348 dicyanocobinamide, 348 isopropylcobinamide, 348 methylcobinamide, 348

tetracarboxylic acid, 415 theoretical considerations, 396 thiocyanatocobalamin, 411 trifluoroethylcyanocobalamin, 413 vibrational components, 403 vinylcobalamin, 346, 350, 415 vinylcobinamide, 408 vinylcyanocobalamin, 413 vitamin B12:

bound to intrinsic factor, 414 chlorination, 215 hexacarboxylic acid, 417 lactam, 417 lactone, 417

pentacarboxylic acid, 417 solvent effects, 207, table, 343, 393-430 vitamin B12 coenzyme: base-on, off, 357 flash photolysis, 299 photolysis, 296

solvent effects, 343, table, 350, 408, 410

vitamin B 12r, 41 8 vitamin B12s, 418

zinc 15 -cyano-2,2,7,7,12,12-hexamethylcorrin, 424 Electronic structure: cobalt(II) complexes, 438 corrinoids, nmr spectroscopy, 487

s-bonded organocorrinoids, vitamin B12

coenzyme, 547 bridged cation, diol dehydrase, 555 cobalt-carbon bond cleavage: homolysis, 456

vitaminB12 coenzyme, 507, 547 cobalt role, vitamin B12 coenzyme, 555 cobalt(II) substrate radical separation,

vitamin B12 coenzyme, 452 5 '-deoxyadenosyl radical, vitamin B12

coenzyme, 554 dihydroxyalkylcobalt complexes, models

for, 572 diol dehydrase: epr spectroscopy, 558 vitaminB12 coenzyme, 529, 546 dissociation-recombination pa hway,

vitamin B12 coenzyme, 555 electron transfer, vitamin B12 coenzyme,

547 epr spectroscopy:

organic radicals, 559 radical doublet intermediates, 450 VitaminB12 coenzyme, 431-462, 558

ethanolamine ammonia-lyase: epr spectroscopy, 558 vitamin B12 coenzyme, 529 vitamin B12r-substrate radical separation, mechanism, 453, 546

glutamate mutase, vitamin B12 coenzyme, 529

glycerol dehydrase, 546 2H intermediates, epr spectrum, vitamin

B12 coenzyme, 450 hydrogen abstraction, vitamin B12

coenzyme, 554 hydrogen exchange, vitamin B12 coenzyme,

449 hypothetical pathways, vitamin B12

coenzyme, 547 kinetic isotope effect, vitamin B12

coenzyme, 554 methylcobalamin, 528 methylmalonyl-CoA mutase, 546

vitamin B12 coenzyme, 529 MO-calculations, vitamin B12 coenzyme,

557 model systems, vitamin B12 coenzyme,

501-541,564-577 organic radicals, vitamin B12 coenzyme,

547 oxidative addition, vitamin B12 coenzyme,

576

Electronic structure (Cont'd) electronic spectrum, conformations, 343 Electron transfer: bis(salicylaldehyde)e hylenediimine-

cobalt(II)(methylimidazole), halogen abstraction, 519

cobalt(I) complexes, alkylation, 259 mechanism, cobalt complexes reductive

arylation, 270 vitamin B12 coenzyme, enzymic reactions,

547 migration of group X, 555

Electrophiles, cobalt-carbon bond, reaction with, 312-317

Electrophilic attack, MO-calculations, vitamin B12, 212

Electrophihc cobalt-carbon bond cleavage, 526

Electrophilic decomposition, alkylcobalamins acid catalyzed, 527

Electrophilic substitution: corrin, 345 MO-calculations, corrin, 212

Electrophoresis, corrin, 249 b-Elimination:

alkylcobaloximes, 364 cobalt-carbon bond, 362 cobalt-carbon bond angles, 369 reversibility, 367

thermolysis, cobalt-carbon bond, 304 vitamin B125, isopropylcobalamin, 364 ENDOR, vitamin B12r, 441, 442 Energerics, cobalt-carbon bond cleavage, 551 Energies, cobalt-carbon bond, 554 Enhancers, epr spectroscopy, 447 Enols, reaction with cobalt(III) complexes, 279 Enzyme bound vitamin B12 coenzyme, 554 Enzymes: corrin biosyn hesis: broken cell, 116 cell free, 116 Enzymic formation: vitamin B12r, 157 vitamin B12s, 158 Enzymic prepara ion, cobinamides, 152 Enzymic reaction: active site thiol, vitamin B12 coenzyme, 555

aminomutases, 546 2-amino-l-propanol, radical intermediates, 450

Epr signals during catalysis, vitamin B12

coenzyme, 332 Epr spectroscopy: alkylcobaloximes, photolysis, 524 angular anomalies, cob(II)inamides, 443

anisotropic hyperfine interaction, cob(II)inamides, 443

carbon-skeleton, 381 cob(II)amides, fifth axial ligands, 444 cobalamins, 433-442 cobalt(II) complexes, 433 cobinamides, 442448 dipolar coupling, 452 enhancers, 447 enzymic reaction:

diol dehydrase, 558 ethanolamine ammonia-lyase, 558 ribonucleotide reductase, 431-462, 558

function of fifth ligand, table, cob(II)- inamides, 444

hyperfine splitting, 436 isomerase reac ions, 381 isotropic exchange, 452 monoclinic model, vitamin B12r, 440 organic radicals, enzymic reaction,

559 powder samples, vitamin B121., 439,

442 principal axes, vitamin B12,., 440 radical doublet intermediates, enzymic

reaction, 450 rapid reaction intermediate, epr

spectrum, 455 single crystals, vitamin B121., 442 theory, 435 vitamin B12 coenzyme, enzymic reaction,

449-458, 558 Epr spectrum: alkylcobaloximes, cation radicals, 517 aquocob(II)inamide, 448 cob(II)inamides, oxygenation, 434, 458 cobalt(II) complexes, organic radical

interaction, 450 cobinamides, steric interactions, 448 5,6-dimethylbenzimidazole, steric

interaction with corrin ring, 448

5,6-dimethylbenzimidazolecob(II)inamide, 448

enzymic reaction: ribonucleotide reductase, 451

Enzymic reaction (Cont'd)

protein role, vitamin B12 coenzyme, 555 radical doublet intermediates, vitamin B12

coenzyme, 450 rapid reaction intermediate, vitamin B12

coenzyme, 455 reaction pathways, vitamin B12 coenzyme,

555 reversibility, vitamin B12 coenzyme, 545 ribonucleotide reductase:

epr spectroscopy, 558 epr spectrum, 451

VitaminB12 coenzyme, 529 table, vitamin B12 coenzyme, 546 theoretical studies, vitamin B12 coenzyme, 557 vitamin B12r as intermediate, vitamin B12

coenzyme, 530 vitamin B12r: intermediate, 381

organic radical interaction, epr spectrum, 450

Enzymic reduction, aquocobalamin, 157 Enzymic role, olefin p-complexes, vitamin

B12 coenzyme, 534 Epicobalamin, see NeovitaminB12

8-Epicobalamin, structure, 225 13-Epicobalamin, structure, 224 3-Epicorrinoids, 224. See also Neocorrinoids 8-Epicorrinoids, 224

biological activity, neocorrinoids, 225 circular dichroism, neocorrinoids, 225 see also Neocorrinoids

13-Epicorrinoids, 224. Seealso Neocorrinoids

Epimerization: equilibrium constants, corrin, table, 222 mechanism, corrin, 224 MO calculations, corrin, 220 neocorrinoids, trifluoroacetic acid, 220,

222 trifluoroacetic acid, corrin, 222

Epimers: corrin, 210 VitaminB12, 210

3-Episirohydrochlorin: absolute configuration, 130 identity with Factor IIa, 129

structure, 129 Episulfides, vitamin B12 total synthesis, 185 Epoxides, reaction with cobalt(I) complexes,

256

Epr spectrum (Cont'd) vitamin B12r, organic radical inter action, 450 epr spectroscopy, rapid reaction inter mediate, 455 high pH, table, cob(II)inamides, 447 nitroalkylcorrins, photolysis, 405 oxygenated vitamin Bnr, 458 ribonucleotide reductase, rapid reaction

intermediate, 455 simulation:

azidocob(II)inamide, 445 histidine cob(II)amide, 445

simulation, cob(II)amides, table, 446 vitamin B12 coenzyme, enzymic reaction:

13 C intermediates, 450 2 H intermediates, 450

vitamin B12r: base-on, off, 299 oxygenation, 458

steric interactions, 434, 439, 442, 448 Equilibria: axial ligands, 345

cobalt-carbon bond, dissociation energy determination, 507

5- and 6-coordinate, table, cobinamides, 350

Equilibrium constants: aquocobalamin, ligand substitution, 337 corrin, epimerization, 220 hydridocobalt complexes, cobalt(I)

complexes, 506 Equilibrium data, cob(II)aloximes, 504 Equilibrium determination, 1-phenylethyl-

(pyridine)cobaloxime, bond dissociation energy, 508

Esr, see Epr spectroscopy; Epr spectrum; Epr signals during catalysis, vitamin B12 coenzyme

Ester ammonolysis, vitamin Bl2 total synthesis, 192

Esterification, basic conditions, vitamin B12

total synthesis, diazomethane, 193

Ethane, methylcobalamin photolysis, 300 Ethane-l,2-diol, see Ethylene glycol Ethanolamine, vitamin B12 coenzyme

photolysis, acetaldehyde, 298, 328

Ethanolamine ammonia-lyase: enzymic reaction, 546 epr spectroscopy, enzymic reaction, 558

epr spectrum, 450 inhibition, nitrous oxide, 373 MO-calculations, 557 model systems, vitamin B12 coenzyme, 571 olefin p-complexes, vitamin B12 coenzyme,

575 radical cations, vitamin B12 coenzyme,

573 radical intermediates, 556 rapid reaction intermediate, 455 reaction pathways, vitamin B12 coenzyme, 555,573 vitamin B12 coenzyme, enzymic reaction,

529 vitamin B12r-substrate radical separation:

mechanism, enzymic reaction, 455 table, 454

1,N6-Ethenadenosine, vitamin B12 coenzyme fluorescent analogs, 300

E heneimine, reaction with cobalt(I) complexes, 257

1 ,N6 -Ethenoadenosylcobalamin, preparation, 267

Ethoxycarbonylcobalamin, al kaline decomposition, 360

2-Ethoxyethylamine, vitamin B12 coenzyme photolysis, acetaldehyde, 298

b-Ethoxyethyl(pyridine) cobal oxime, ethylene, a cid decompo sition, 313

Ethylcobalamin: electronic spectrum, 408 nmr spectrum, 468, 474 photolysis, 302 solution thermolysis, 304 spin-lattice relaxation times, 492 Ethylcobinamide: deuteration, 345 electronic spectrum, 408 Ethylcyanocobalamin, electronic spectrum, 413 Ethylene: acid decomposition: b-ethoxyethyl(pyridine) cobaloxime, 313 methoxyethylcobalamin, 313 hydroxyethylcobalamin, acid decomposi tion, 313 Ethylene glycol: acetaldehyde, methyl(aquo)cobaloxime

photolysis, 571 pulse radiolysis, acetaldehyde, 574

electronic spectrum, vitamin B12 coenzyme, 299

methylcobalamin, 300, 335, 363, 525, 553

methylcobaloxime, 405 methylcobalt complexes, 525 vitamin B12 coenzyme, 376

Fluorescence spectrum: cobalt-free corrin, 402, 422 vitamin B12,426

Fluorescent analogs: 2,6-diaminobulorine, vitamin B12

coenzyme, 300 formycin, vitamin B12 coenzyme, 300 1,N6 -ethenadenosine, vitamin B12

coenzyme, 300 vitamin B12 coenzyme, 267, 285 Fluxionality, cobalamins, nmr spectroscopy, 490 FMN, cobalamin reduc ion, 157 FMNH2 , methionine biosynthesis, 162 Folding, corrin derivatives, 59 Formal oxidation state, alkylcobalt

complexes, 514 Formate reduction, diaquocobinamide,

447 Formycin, vitamin B12 coenzyme

fluorescent analogs, 300 Formycinylcobalamin, preparation,

267 Formycyclobalamin, reaction with cyanide, 307 Formylmethylcobalamin: preparation, 283, 315 reaction with acid, 314 Formylmethylcobaloxime, preparation, 315 Frozen solution epr, vitamin B12 coenzyme

photolysis, 299

Gadolinium(III), shift reagent, corrin ring, 472,482 GCoPSE: preparation, yellow corrinoids, 40 structure, yellow corrinoids, 42 X-ray diffraction data, yellow corrinoids, 40

see also Yellow corrinoids Glossary, X-ray crystallography, 97 Glutamate mutase:

acrylate radical, vitamin B12 coenzyme, 571

enzymic reaction, 546

Ethylene glycol (Cont'd) vitamin B12 coenzyme, photolysis,

acetaldehyde, 298, 328 Ethyl vinyl ether, reaction with cobalt(III)

complexes, 281 Ethynylcobalamin, electronic spectrum,

411,415 Euglena gracilis, corrin, biosynthesis,

117 Eukaryotes: cobalt-carbon bond, biosynthesis, 155-163 vitamin B12 coenzyme, biosynthesis, 156-161 1 H/ 2H exchange: corrin ring, nmr spectrum, 469 nmr spectrum, vitamin B12 coenzyme, 468,469 Extraction, corrins by phenol, 249

Factor A: nomenclature, 17 X-ray crystallographic data, 92

Factor I: biosynthesis, 131 electronic spectrum, 130 incorporation into cobyrinic acid, 131 isolation from C. tetanomorphum, 130 isolation from P. shermanii, 130 reduced form incorporation into:

cobyrinic acid, 131 tetrahydrochlorin, 131

structure, 130, 131 Factor II, see Sirohydrochlorin Factor IIa:

3-episirohydrochlorin, identity with, 129

see also 3-Episirohydrochlorin Factor III:

5-methoxybenzimidazole, 471 nmr spectrum, 471, 472

Factor Via, see Cobyric acid FAD, cobalamin reduction, 157 Ferredoxin:

corrin reduc ion, 254 decyanation, vitamin B12, 163

Fifth axial ligands, epr parameters, table, cob(II)amides, 444

First crystallization, vitamin B12, 3 Five coordinate:

cobalt(III) complexes, stable, 506 decomposition, alkyl cobalamins, 369

Flash photolysis: alkylcobalt complexes, 525

Glutamate mutase (Cont'd) glycinyl radical, vitamin B12 coenzyme, 571 model systems, vitamin B12 coenzyme, olefin p-complexes, vitamin B12 coenzyme, 571 radical intermediates, 556 reac ion pathways vitamin B12 coenzyme, 571 vitamin B12 coenzyme, enzymic reaction,

529 L-Glutamic acid, 328 Glutathione, nucleotide loop biosynthesis,

cofactor, 152 Glyceraldehyde, photolysis, dihydroxy-

propylcobalamin, 302 Glyceric acid, photolysis dihydroxypropyl-

cobalamin, 302 Glycerol dehydrase, enzymic reaction, 546 Glycerol photolysis, dihydroxypropyl-

cobalamin, 302, 328 Glycinyl radical, vitamin B12 coenzyme,

glutamate mutase, 571 N-Glycosides: biosynthesis, enzyme isolation, 153 cobalamins, configurations, 153 Glyglycobalamin, reac ion with, hydroxy-

lamine, 312 Gold(I), alkylcobalt complexes, alkyla-

tion, 527 Grignard reagent: cobalt(III) complexes, alkylation, 277,

517 phenyl(pyridine)cobaloxime, preparation,

278 Group participation effects, f-amide cleavage,

235 Guanosine diphosphate:

cobinamide phosphate, addition of, 151 cobinamides nucleotide loop, biosyn thesis, 152

H2/Pt, reductive cleavage, methylcobalamin, 317 Hagemann's ester, vitamin B12 total syn thesis, 184 Haloenzyme synthetase, 163 Halogen abstraction: alkyl halides, cobalt(II) complexes, 519 cobalt(II) complexes, 274 electron transfer, bis(salicylaldehyde)- ethylenediiminecobalt(II)- methylimidazole, 520

Halogenation: cis-effect, vitamin B12, 216 corrin, 204, 215 lactam formation, 226 lactone formation, 226 me hylcobalamin, 216 sulfonatocobalamin, 216 vitamin B12, 226 VitaminB12 coenzyme, 216

Halogen cleavage: alkylcobaloximes, 317 benzylcobaloxime, 317 isopropylcobaloxime, 317 stereochemistry, cobalt-carbon bond,

317 Halogens, cobalt-carbon bond cleavage,

516,526 Halomethylcobaloximes, reaction with

alkali, 308 Halomethylcobalt porphyrins, diazomethane,

preparation, 280 Heavy metal methylation, methylcobalamin,

528 Helicity: corrin, 209 vitamin B12, 209 Heptamethylcob yrinate: coordination, l-(2-trifluoromethylphenyl)-

imidazole, 495 iodide complex, structure, 72 reaction with methylmagnesium iodide, 278 see also Heptamethylcobyrinic acid

Heptamethylcobyrinic acid: 13Cnmr, 112 degradation, 113 ozonolysis, 115 structure, 114

Heptamethyl dicyano-5,15-bisnorcobyrinate: preparation, 239 vitamin B12, conversion to,

239 Heptamethyl dicyano( 10-bromocobyrinate),

ozonolysis, 218 Heptamethyl dicyanocob yrinate:

preparation, 236 reduction to heptanol, 226, 237 vitamin B12 , conversion to, 236

Heterolytic cleavage: alkyIcobalamins, 305-319 alkylcobaloximes, 305-319 cobalt-carbon bond, vitamin B12 coenzyme,

305-319,548

Hexacarboxylic acid (vitamin B12): bond angles, tables, 45-53 bond distances, tables, 45-53 cell dimensions, 92 chemical formula, 92 deuteration, 212 electronic spectrum, 417 folding, 60 space group, 92 structure, 28, 204 torsion around A-D junction, 57 X-ray crystallographic data, 92 X-ray diffraction data, 27 X-ray structure, 31, 32

see also Vitamin B12

Hexachloroiridate, oxidation, alkylcobaloximes, 515, table, 516 5,7,7,12,14,14-Hexamethyl-l,4,8,ll-

tetraazacyclotetradeca-4,11-dienecobalt:

alkyl complexes, 271 structure, 574 vitamin B12 coenzyme, model systems,

574 High pH, cob(II)inamides, epr spectrum,

447 High pressure liquid chromatography,

vitamin B12 total synthesis, 190 Histidine cob(II)amide, epr spectrum

simulation, 445 History, vitamin B12, 1 Homocysteine: S-adenosylhomocysteine, from vitamin

B12 coenzyme and, 298 methylation, methylcobalamin, 528 methylcobaloxime, me hylation, 529 Homolytic cleavage: cobalt-carbon bond: activation enthalpy, 511 vitamin B12 coenzyme, 296, 362, 548 5-coordinate, 371 thermolysis, neopentylcobalamin, 364 Hydrated electrons, reaction with corrin, 318 Hydrazines and oxygen:

cobaloximes, alkylation, 275 cobalt complexes, alkylation, 275

1,2-Hydride shift, vitamin B12 coenzyme, 549

Hydrides: cobalt, 365 pK values, cobalt, 335 stability, cobalt, 335

Hydridocobalamin: bond dissociation energy, 507 electronic spectrum, 365 pKa values, 506 preparation, 253, 365 secondary alkylcorrinoids, preparation, 552 vitamin B12 coenzyme, 549

Hydridocobaloxime, 252 Hydrido(pyridine)cobaloxime, bond dissociation energy, 507 Hydrido(trwz-butylphosphine)cobaloxime: bond dissociation energy, 507 olefin addition, radical intermediates, 518 pKa values, 506 preparation, 253 Hydridocobalt complexes: acidity, 253,506 addition to olefins, mechanism, 265 bond dissociation energy, 506 cobalt(I) complexes, equilibrium, 506 Hydridopentacyanocobalt: acidity, 253

addition to olefins, mechanism, 263 bond dissociation energy, 507 olefin addition, free radical intermediates, 518

pKa values, 506 Hydrogen abstraction: 5 '-deoxyadenosine, 554 vitamin B12 coenzyme enzymic reaction, 554 Hydrogen cyanide, vitamin B12 coenzyme

reaction with, 306 Hydrogen exchange: with solvent, ribonucleotide reductase,

449 vitamin B12 coenzyme enzymic reaction,

449 Hydrogen perox ide, corrin ox idation, 218 Hydrogen reduc ion, cobaloximes, cobalt

complexes, 252 Hydrolysis: acid, amide groups (corrin periphery),

33,230,234 alkyl(pyridine)cobaloximes, cation

exchange resin, 249 Hydrophobic pocket, vitamin B12 coenzyme.

41 Hydroxocobalamin:

alkylation, vinyl ethers, 281 electronic spectrum, 404, 417

b-Hydroxy-n -propylpyridinatocobaloxime: b-hydroxy-isopropylpyridinatocobaloxime, acid catalyzed rearrangement to, 314 reaction with acid, 314

4-Hydroxy-2,2,6,6-tetramethylpiperidine- N-oxylcobamide coenzyme, preparation, 267

Hyperfine splitting, epr spectroscopy, 436 Hypothetical pathways, vitamin B12 co-

enzyme, enzymic reactions, 547

Imidazole, coordination to alkylcorrins, 358

Imidazolecobalamin, electronic spectrum, 411

Incorporation into: C tetanomorphum, sirohydrochlorin, 123 cobyric acid, trimethylated isobacterio-

chlorins, 132 cobyrinic acid:

Factor I, 131 sirohydrochlorin, 123

corrin: 5-aminolevulinic acid, 111 methionine, 111 porphobilinogen, 111 15-cyano-l ,2,2,7,7,12,12-heptamethyl-

corrin, metals, 211 vitamin B12: cobalt, 211 copper, 211 rhodium, 211 zinc, 211 Infrared spectrum: lactones (corrin ring), 228 vitamin B12, 215 Inhibition: nitrous oxide: diol dehydrase, 373 e hanolamine ammonia-lyase, 373 nitial isolation, hydroxocobalamin, 12 Insertion of dioxygcn, cobalt-carbon bond, 512 Interaction with:

corrin p-orbitals, cobalt orbitals, 561 corrin ring: 5 '-deoxyadenosyl ligand, 66 5,6-dimcthylbenzimidazole, 353 cosynthetase, uroporphyrinogen I, 118 substrate radicals, vitamin B12r-, inter-

mediate, 382

Hydroxocobalamin (Cont'd) initial isolation, 12 nmr spectrum, 468, 474 nomenclature, 17

see also Aquocobalamin Hydroxyalkylcobaloximes, reaction with acid, 313 2-Hydroxyalkylcobaloximes, preparation,

reac ions, 284 b-Hydroxyalkylcobaloximes, reaction with

alkali, 310 a-Hydroxyalkylcobalt complexes, prepara tion, pulse readolysis, 273 4-Hydroxy-n-butylcobaloxime, reaction

with acid, 314 10-Hydroxycobalamin, 217 trans-2-Hydroxycyclohexylcobaloxime, reaction with alkali, 311 b-Hydroxye hylaquocobaloxime, decomposition in acid, 313 Hydroxyethylcobalamin: acid decomposition, ethylene, 313 reaction with alkali, 311 spin-lattice relaxation times, 492 2-Hydroxyc hylcobaloximes: acid catalyzed decomposition, 518 olefin p-complexes, acid catalysis, 575 reaction with alkali, cob(I)aloxime, 310 Hydroxyethylcobinamide, reaction with alkali, 311 Hydroxycthylcyanocobalamin, electronic

spectrum, 413 2- Hydroxyethyl vinyl ether, reaction with

cobalt(III) complexes, 282 b-Hydroxyisopropylcobaloxime, reaction

with hydroxide, 310 b-Hydroxyisopropyl(pyridine) cobaloxime: acid catalyzed rearrangement to 0-hydroxy-

n -propylpyridinatocobaloxime, 314 photolysis, 302 Hydroxylamine: acetylcobalamin, reaction with, 312 acetylglycobalamin, reaction with, 312 glyglycobalamin, reaction with, 312 b-Hydroxypropionaldehyde, 328 b-Hydroxypropylcobaloximcs, acetone, photolysis, 302 b-Hydroxy-/i-propyl(pyridinc)cobaloxime, preparation, 257 3- Hydroxy-rt -propylcobaloxime, reaction with acid, 314 |3-Hydroxy-H-propylcobaloximc, reaction with hydroxide, 310

Isomerase reactions: basic schemes, 375 carbonium ion mechanism, 377 epr spectroscopy, 381 neopentylcobalamin as model, 375 proposed mechanisms, 383 vitamin B12, dependent, table, 328,

330-333 a,b-Isomers: corrin, circular dichroism, 421 electronic spectrum, cobinamides, 413,

table, 416 methylcobinamide, nmr spectroscopy

(13C), 484 nmr spectrum, cyanoaquocobinamide,

484 Isopropylaquocobaloxime, redox potential,

516 Isopropyl bis(acetylacetone)ethylenediiminecobalt, radical scavengers, thermal decomposition, 512 Isopropylbis(salicylaldehyde)ethylenediiminecobalt, radical scavengers, thermal decomposition, 512 Isopropyl bis(salicylaldehyde-o - phenylenediimine)cobalt, radical scavengers, thermal decomposition, 512 Isopropylcobalamin: electronic spectrum, 255, 408 b-elimination, vitamin B128, 364 pH decomposition rates, 370 rate of acid catalyzed decomposition, 371 thermolysis: base-on, off, 552 kinetics, 552 Isopropylcobaloxime: cobalt-carbon bond: bond dissociation energy, 511 length, 359 halogen cleavage, 317 Isopropylcobinamide, electronic spectrum, temperature variation, 255, 348, 408 2', 3 -Isopropylidcneadenosylcobalamin

and r-butoxide, vitamin B128, 307 2',3'-O-Isopropylidenecy clodihydrouridine: formation, 297 structure, 298 2', 3 '-Isopropylidene-5 '-deoxy-(D)ribosyl- cobinamide, nmr spectrum, 486 2', 3 '-O-Isopropylidene-5 '-deoxy-8,5 '- cyclonucleosides, 300

Interconversion: cobalamin coenzymes, 163 sirolactone, sirohydrochlorin, 123 Intermediate, enzymic reaction: vitamin B12r, 381 vitamin B12 coenzyme, 5'-deoxyadenosine, 332 Intramolecular 1,2-shifts, organic radicals, 556 Intramolecularly bridged cobaloximes,

269 Inversion of configuration, methionine

methyl transfer, 115 Iodide:

heptamethylcob(II)yrinate, dimeric complex with, 522

vitamin B12r, complex with, 522 Iodine: cleavage: me hylcobalamin, 316 stereochemistry, (S)-me hylheptyl- pyridinatocobaloxime, 317 vitamin B12 coenzyme, 316 lactone formation, vitamin B12, 226 Iodocobalamin, electronic spectrum, 411 Iodocobalt(II) [cobyrinic acid-a,b,c,d,e,f,g- heptamethyl ester] dimer: cell dimensions, 95 chemical formula, 95 space group, 95 X-ray crystallographic data, 72, 95 Ion exchange chromatography, corrin, 249 Ionization energies, metals, 331 Iron alkyl bond, 331 7-Irradiation, frozen solution:

vitamin B12, 318 vitamin B12 coenzyme, 318 3-Isoadenosylcobalamin, acid cleavage, 312 Isobacteriochlorins:

sulfite and nitrite reductases, 122 synthesis, 122, 135

see also Sirohydrochlorin; Sirolactone Isolation: C tetanomorphum, Factor I, 130 corriphyrin-3, 134 corriphyrins, 121, 122 desulfoviridin, sirohydrochlorin, 122 P. Shermanii t Factor I, 130 sirohydrochlorin, P. shermanii, 122 trimethylated isobacteriochlorins, 132 vitamin B12, 3, 24

2', 3'-O-Isopropylidene-5 '-deoxyuridyl- cobalamin, photolysis, 297 Isopropyl(pyridine)bis(salicylaldehyde-o- phenylenediimine)cobalt, bond dissociation energy, 512 Isopropyl(pyridine)cobaloxime, cobalt- carbon bond, bond lengths, 505 Isopropyl(tricyclohexylphosphine) cobaloxime: cobalt-carbon bond, bond leng hs, 506 nmr spectrum, 506 Isopropy l(triphenylphosphine) cobaloxime: cobalt-carbon bond, bond leng hs, 505 nmr spectrum, 506 Isotropic exchange, epr spectroscopy, 452 Isoxazoles, vitamin B12 total synthesis, 175

Kinetic isotope effect: [I-2H2 ] propane-l,2-diol, vitamin B12

coenzyme, 554 vitamin B12 coenzyme, enzymic reaction, 554 Kinetics: cobaloximes, alkylation, 259 cobalt-carbon bond: activation en halpy, 511 dissociation energy determination, 511 cobalt(I) complexes, alkylation, 258 cyclopropylcarbinyl radical rearrange ments , 567isopropylcobalamin thermolysis, 552 vitamin B12s alkylation, 259 Kramer's doublets, 435

13C-Labelled: alkylcobalamins, 268 cobalamins, 474 corrin, 474 2H-Labelled, vitamin B12 coenzyme, 5'-

methylene group, 545 3H-Labelled, vitamin B12 coenzyme, 5'- methylene group, 545 Labilization by: protein, cobalt-carbon bond, 333 steric interactions, cobalt-carbon bond, 361 Lack of aromaticity, corrin, 204 Lactam formation: corrin, cyclization (peripheral), 225-230, 234

halogenation, 226 methylcobalamin, 226 sulfonatocobalamin, 226 vitamin B12, 225, 234 vitamin B12 coenzyme, 226

Lactams (corrin ring): biological activity, 225 electronic spectrum, vitamin B12 , 417 formation, mechanism, 226 c-lactam forma tion, 23 4

Lactobacillus leichmanni: cobalamin biosynthesis, 160

ribonucleotide reductase, vitamin Bnr

formation, 439 Lactone formation:

corrin, cyclization (peripheral), 225-230 halogenation, 226 iodine, 226 vitamin B12, 226

Lactones (corrin ring): electronic spectrum, vitamin B12, 417 infrared spectrum, 227 mechanism of forma ion, 225-230 preparation, 226 spiro, 227

Lanthanide shift reagents: corrin ring, nmr spectrum, 471, 482 nmr spectrum, carboxymethylcobalamin,

472 Laser Raman spectrum, corrin derivatives,

343 LCAO-MO, electronic spectrum, 396 Lead(II):

alkylation, trans-dimethylcobalt(III) complexes, 527

cobalt-carbon bond, 54 a-Leucine, (R)-2,5-diaminopentanoate,

546 LiAIH4, heptamethyl dicyanocobyrinate

reduction, 237 Ligand binding, vitamin B12 coenzyme

model systems, 504 Ligand equilibria, vitamin B12 coenzyme

steric effects, 341 Ligand exchange:

alkylcobalamins, steric effects, 341 5 ,6-dimethylbenzimidazole, thermodynamics, 496

Ligand modification, alkylcobalt complexes, 283-286

Ligand ordering, trans-effect, 346 Ligand substitution: corrin, 330, 337

Ligand substitution (Cont'd) equilibrium constants, table, aquo-

cobalamin, 337 Ligands, s-donor power, 333 Lithium, incorporation into 15-cyano-

1,2,2,7,7,12,12 -heptamethylcorrin, 21 i

Longitudinal relaxation times, vitamin B12, nmr spectrum, 485

Loss of C-20 in corrin biosynthesis, 137 Low spin Co(II), vitamin B12r, 432 Luminescence:

cobalt-free, corrinoid, 426 corrin, 426 vitamin B12,426

D-a-Lysine, 328 L-b-Lysine, 328

Macrocycle reactions, corrin, 201-243 Magentic circular dichroism: cobalt 15-cyano-7,7,12,12,19-penta-

methylcorrin, 424 cobalt-free corrin, 423 cob(II)inamides, 426 copper cobalamin, 426 dicyanoheptamethylcobyrinate, 426 metallocorrins, 424 nickel 15 - cy ano - 7,7,12,12,19 - pen ta-

methylcorrin, 424 nickel 7,7,12,12,19 -pentamethylcorrin , 424 Magic Mannich, dimethylaminomethylation

of corrin, 213 Magnetic properties, corrin, 330 Malononitrile, reaction with cobalt(III) complexes, 279 Mammalian: biosynthesis, methylcobalamin, 163 methionine synthetase, 163 MCD, see Magnetic circular dichroism Me6[14]diene N4,see 5,7,7,12,14,14- Hexamethyl-1,4,8,11 -tetraazacyclotetradeca-4,11-dienecobalt; Cobalt complexes Mechanism: alkynes, addition, 263 carbon-skeleton, 385 cobaloximes, addition to olefins, 264 cobalt complexes, reductive arylation

electron transfer, 270 cobalt(I) complexes, addition to

olefins, 265 corrin epimerization, 220

enzymic reaction, ethanolamine ammonia- lyase, vitamin B12 ,.-substrate radical separation, 453

hydridocobalt complexes, addition to olefins, 265

hydridopentacyanocobalt, addition to olefins, 263

lactams (corrin ring), formation, 225 methionine, methyl transfer, 113 model systems, 383 olefins, addi ion to cobalt(I) complexes,

262 reductive alkylation, cobalt complexes,

254-270 role of model systems, vitamin B12

coenzyme, 528 vitamin B12 coenzyme, methylmalonyl-CoA

mutase, 565 Mechanism of ac ion: model systems, vitamin B12 coenzyme,

543-582 theory, vitamin B12 coenzyme, 543-582 Mechanism of formation: dehydrocobinamide, 226 yellow corrinoids, 39, 229 Me[14]-diene N4: pulse radiolysis, 574 structure, 574 Mercaptides: alkylcobaloximes, reaction with, 311 methyl(aquo)cobaloxime, reaction with 311 Mercury(II): alkylation: alkylcobaloximes, 526 alkylcobalt complexes, 526 methylpentacyanocobaltate(III), 5 26 cobalamins, coordination, 495 cobalt-carbon bond cleavage, 526 methylation, methylcobalamin, 529 methylcobalamin alkylation, 526 methylpentacyanocobalate(III), 529 stereochemistry, alkylcobalt complexes, 526 Meso-substitution, corrin, 212 Metal complexes, secocorrins, X-ray crystal-

lographic data, 77, 96 Metal-free:

electronic spectrum, corrin, 207, 395 vitamin B12, 211

Metal ions: adenosyla ing enzyme, 161 cobalamins, reaction with, 495

Metallation: corrin, 210-212 15-cyano-l,2,2,7,7,12,12-heptamethyl-

corrin, 211 descobaltocobalamin, 211 descobaltocobamide, 211

15 -cy ano -1,2,2,7,7,12,12 - heptamethylcorrin, 211 Metal-Iigand bond angles, 46 Metal-Iigand bond lengths, 45 Metallocorrins:

deuteration, 220 electronic spectrum, 424

magnetic circular dichroism, 424 Metalloenzyme chemistry, 326 Metalloporphyrins, cobalt-carbon bond, 246 Metal replacement, vitamin B12, 72 Metals:

ionization energies, 331 methylation, methylcobalamin, 528 Methane biosynthesis, methylcobalamin, 528 Methane formation, hydroxide and methyl(aquo)cobaloxime, 308 Methanolysis, vitamin B12, 236 Methanosarcina barkeri, methylcobalamin

biosynthesis, 162 Methionine: biosynthesis: FMNH2, 162 NADPH, 162 chiral methyl, 115 incorporation into: corrin, 111 13C, 112 methylation, stereochemistry, 113 methyl transfer: inversion of configuration, 115 mechanism, 113 Methionine formation, S-adenosylmethionine, 329 Methionine synthetase: activation, 162 mammalian, 163 [13CH3 ]-L-Methionine: vitamin B12 biosynthesis, 480 CD3-methyl incorporation into: corrin, 114 I ntact transfer, 114 8-Methoxyadenosylcobalamin, 298 5-Methoxybenzimidazole, Factor III, 471

Methoxycarbonylethylcobalamin, reaction with alkali, 310

Methoxyethylcobalamin ethylene, acid decomposition, 313

Methylacrylate, addition to cobalt(I) complexes, 256 Methyl(aquo)cobaloxime: cobalt-carbon bond, bond lengths, 505 methane formation, hydroxide, 308 photolysis, acetaldehyde, 571 reaction with: acid, 313 mercaptides, 311 redox potential, 516 Methyl(aquo)cobyrinic hepta terf-alcohol: preparation, 278 structure, 278 threo-b-Methylaspartic acid, 328 Methylation: homocysteine, methylcobaloxime, 529 methylcobalamin: homocysteine, 528 mercury(II), 529 metals, 528 N5 methyltetrahydrofolic acid, vitamin B12

528 stereochemistry, methionine, 113

1-Methylbilane, corrin biosynthesis, 121 2- Me hyl-2-butylcobalamin, rate of, 371 1-Methylbut-3-enyl(pyridine)cobaloxime,

rearrangements,2-methylbut-3- enyl(pyridine)cobaloxime, 569

2- Methylbut-3-enyl(pyridine)cobaloxime, 1-methylbut-3-enyl(pyridine)- cobaloxime, rearrangements, 569 Methylcobalamin: alkylation, mercury(II), 526 biosynthesis: Clostridium thermoaceticum, 161 E. Coli f 161

Methanosarcina barkeri, 162 NADPH, 162 Streptomyces griseus, 161-163

carbon dioxide, reduction to, 528 circular dichroism, 420 complex with, Z>w-acetylacetone-

ethylenediamine, X-ray structure, 349

13C containing, 268, 301, 326 conversion to vitamin B12 coenzyme, 163 coupling constants 13C-H, 490 dimcthylmercury(II), 526

nmr spectroscopy (13C), a, j3-isomers, 484

Methylcorrinoids: trans-effect, nmr spectroscopy, 489 a ,b, photoisomerization, 301 Methylcyanocobalamin: electronic spectrum, 413 nmr spectrum, 468 3-Methylcyclopropylcarbinyl(pyridine)- cobaloxime rearrangements, 1- methyl-but -3-enyl(pyridine)- cobaloxime, 569 l-Methyl-2,2-diphenylcyclopropyl-

(pyridine)cobaloxime preparation, 254

N-Methyleneaniline(pyridine)cobaloxime preparation, 258

a-Methyleneglutarate mutase: model systems, vitamin B12 coenzyme,

567 radical intermediates, 557 reaction pathways, vitamin B12 coenzyme, 570

a-Methyleneglutaric acid, 328 a-Methylene mutase, model systems, 532 1-Methyl-heptylcobaloxime, cobalt-carbon

bond, bond dissociation energy, 511

(S)-Methylheptylpyridinatocobaloxime, iodine cl eavage, ste reochemistry, 317

Methylisocyanatocobalamin, electronic spectrum, 411

b-Methylitaconic acid, 328 Methylmagnesium iodide, heptamethylcobyrinate reaction with, 278 L-Methylmalonyl-CoA, 328 Methylmalonyl-CoA mutase: carbanion intermediates, 556 enzymic reaction, 546 mechanism, vitamin B12 coenzyme, 565

MO-calculations, 557 model systems, vitamin B12 coenzyme,

532,564 reaction pathways, vitamin B12 co-

enzyme, 565,566 vitamin B12 coenzyme, enzymic reac-

tion, 529 Methylmercaptide, methylcobalamin

reaction with, 311 Methylmercury isopropoxide, vitamin B12

total synthesis, 185

Mcthylcobalamin (Cont'd) electrochemical oxidation, 517 electrochemical reduction, 318 electronic spectrum, 408, 415 enzymic reaction, 528 flash photolysis, 300, 335, 363, 525, 553 H2/Pt, reductive cleavage, 317 halogenation, 216 heavy metals, 528 homocysteine, methylation, 528 iodine, cleavage, 316 lactam formation, 226 mammalian, biosynthesis, 163 mercury(Il), methylation, 529 metals, methylation, 528 methane, biosynthesis, 528 methyl transfer, thiols, 312 monomethylmercury(II), 526 nmr spectrum:

pH dependence, 494 praseodymium, 471, 474, 483

nomenclature, 21 photolysis: ethane, 300 methyl radicals, 300 vitamin B12r, 300, 362,404 rate of decomposition, 368 reaction with methylmercaptide, 311 spin-lattice relaxation times, 492 thermolysis, 303, 363 vitamin B12 coenzyme:

conversion to, 163 ratio, 161

see also Alkylcobalamins; Alkylcorrins; Cobalt-carbon bond Methylcobaloxime:

cob(II)aloximes, photolysis, 301 cyanide, acetonitrile formation, 307 flash photolysis, 405 methyla ion, homocysteine, 529 nmr spectrum (59Co), 490 photolysis, methylperoxocobaloxime,

301,553 see also Methyl(aquo)cobaloxime

Methylcobalt complexes: bond lengths, nmr spectroscopy, 506 flash photolysis, 525

Methylcobinamidc: electrochemical reduction, 318 electronic spectrum, temperature varia-

tion, 343, 348,408 13C-enriched, 484

Methylpentacyanocobalate(III), mercuric chloride alkylation, 526

Methylperoxocobaloxime, methylcobaloxime photolysis, 553

l-Methyl-2-phenylethylcobaloxime, cobalt- carbon bond, bond dissociation energy, 511

Methyl(pyridine)bis(acetylacetone)- ethylenediiminecobalt, cobalt- carbon bond, bond lengths, 505

Methyl(pyridine)cobaloxime, cobalt-caxbon bond, bond lengths, 505

Methyl radicals: methylcobalamin photolysis, 300 reactions, 300 recombination: cob(II)alamin, 511 with cobalt(II) complexes, 335 vitamin B12r, 553 scavenger, vitamin Bur, 300 N5 -methyltetrahydrofolic acid, vitamin B125 methylation, 528 Methyl transfer: Inversion of configuration, methionine, 115 mechanism, methionine, 113 thiols, methylcobalamin, 312 Methyltransferase enzyme: properties, 135 purification, 135 Methyl(triphenylphosphine) cobaloxime, cobalt-carbon bond, bond lengths, 505 Microbiological assay, vitamin B12, 7 Microbiological formation, yellow

corrinoids, 228 Migration of group X, electron transfer,

vitamin B12 coenzyme, 555 MO-calculations: aminomutases, 557 corrin:

electrophilic substitution, 212 epimerization, 220 diol dehydrase, 557 ethanolamine ammonia-lyase, 557 methylmalonyl-CoA mutase, 557 vitamin B12 coenzyme, enzymic

reac ion, 557 vitamin B12, electrophilic attack, 212 Model for corrin, cobaloximes, 419 Model for ethanolamine ammonia-lyase,

vitamin B12 coenzyme photolysis, 196

Model systems: bis(salicylaldehyde)ethylenediiminecobalt, vitamin B12 coenzyme, 551 cobalt role, 378 diol dehydrase, 532 ligand binding, vitamin B12 coenzyme, 504 mechanism, 383 methylmalonyl-CoA mutase, 532 pKa values, vitamin B12 coenzyme, 504 redox chemistry, vitamin B12 coenzyme,

504 redox potential, vitamin B12 coenzyme,

504 vitamin B12 : comparison to, 504 redox chemistry, 513 vitamin B12 coenzyme: alkylcobalt complexes, 551, 564 aminomutases, 571 bis(salicylaldehyde)ethylenediimine-

cobalt(III), 551 capped cobaloximes, 533, 565 cobalt-carbon bond cleavage, 551 comparison to, 504 diol dehydrase, 571 enzymic reaction, 501-541, 564-577 ethanolamine ammonia-lyase, 571 glutamate mutase, 570 mechanism, role of, 528 mechanism of action, 543-582 a-methyleneglutarate mutase, 377, 501-541,567

methylmalonyl-CoA mutase, 564 redox chemistry, 513 Modified cobalamins, cobalt-carbon bond

cleavage, 65 Molecular orbitals, bridged cation, 555 p-Molecular orbitals, corrin, 397 Molecular rearrangements, vitamin B12

coenzyme, 545 Molecular structure in solution, com parison to X-ray structure by nmr spectroscopy, 482 Mono-C-methylated chlorin, structure, 131 Monocarboxylic acid, vitamin B12:

bond angles (tables), 45-53 bond distances (tables), 45-53 cell dimensions, 93 chemical formula, 93

nmr spectroscopy (13 C), a,0-isomers, 484

Methylcorrinoids: trans-effect, nmr spectroscopy, 489 a,|b, photoisomerization, 301 Methylcyanocobalamin: bbelectronic spectrum, 413 bbnmr spectrum, 468 3-Methylcyclopropylcarbinyl(pyridine)- cobaloxime rearrangements, 1- methyl-but -3-enyl(pyridine)- cobaloxime, 569 l-Methyl-2,2-diphenylcyclopropyl-

(pyridine)cobaloxime preparation, 254

N-Methyleneaniline(pyridine)cobaloxime preparation, 258

a-Methyleneglutarate mutase: model systems, vitamin B12 coenzyme,

567 radical intermediates, 557 reaction pathways, vitamin B12 coenzyme, 570

a-Methyleneglutaric acid, 328 a-Methylene mutase, model systems, 532 1 -Me hyl-heptylcobaloxime, cobalt-carbon

bond, bond dissociation energy, 511

(S)-Methylheptylpyridinatocobaloxime, iodine cl eavage, ste reochemistry, 317

Me hylisocyanatocobalamin, electronic spectrum, 411

b-Methylitaconic acid, 328 Methylmagnesium iodide, heptamethylcobyrinate reaction with, 278 L-Methylmalonyl-CoA, 328 Methylmalonyl-CoA mutase: carbanion intermediates, 556 enzymic reaction, 546 mechanism, vitamin B12 coenzyme, 565

MO-calculations, 557 model systems, vitamin B12 coenzyme,

532,564 reaction pathways, vitamin B12 co-

enzyme, 565,566 vitamin B12 coenzyme, enzymic reac-

tion, 529 Methylmercaptide, mcthylcobalamin

reaction with, 311 Methylmercury isopropoxide, vitamin B12

total synthesis, 185

Mcthylcobalamin (Cont'd) electrochemical oxidation, 517 electrochemical reduction, 318 electronic spectrum, 408, 415 enzymic reaction, 528 flash photolysis, 300, 335, 363, 525, 553 H2/Pt, reductive cleavage, 317 halogenation, 216 heavy metals, 528 homocysteine, methylation, 528 iodine, cleavage, 316 lactam formation, 226 mammalian, biosynthesis, 163 mercury(Il), methylation, 529 metals, methylation, 528 methane, biosynthesis, 528 methyl transfer, thiols, 312 monomethylmercury(II), 526 nmr spectrum:

pH dependence, 494 praseodymium, 471, 474, 483

nomenclature, 21 photolysis: ethane, 300 methyl radicals, 300 vitamin B121., 300, 362,404 rate of decomposition, 368 reaction with methylmercaptide, 311 spin-lattice relaxation times, 492 thermolysis, 303, 363 vitamin B12 coenzyme:

conversion to, 163 ratio, 161

see also Alkylcobalamins; Alkylcorrins; Cobalt-carbon bond Methylcobaloxime:

cob(II)aloximes, photolysis, 301 cyanide, acetonitrile formation, 307 flash photolysis, 405 methyla ion, homocysteine, 529 nmr spectrum (59Co), 490 photolysis, methylperoxocobaloxime,

301,553 see also Mcthyl(aquo)cobaloxime

Methylcobalt complexes: bond lengths, nmr spectroscopy, 506 flash photolysis, 525

Methylcobinamidc: electrochemical reduction, 318 electronic spectrum, temperature varia-

tion, 343, 348,408 13C-enriched, 484

Methylpentacyanocobalate(III), mercuric chloride alkylation, 526

Methylperoxocobaloxime, methylcobaloxime photolysis, 553

l-Methyl-2-phenylethylcobaloxime, cobalt- carbon bond, bond dissociation energy, 511

Methyl(pyridine)bis(acetylacetone)- ethylenediiminecobalt, cobalt- carbon bond, bond lengths, 505

Methyl(pyridine)cobaloxime, cobalt-carbon bond, bond lengths, 505

Methyl radicals: methylcobalamin photolysis, 300 reactions, 300 recombination: cob(II)alamin, 511 with cobalt(II) complexes, 335 vitamin B12r, 553 scavenger, vitamin B121., 300 N5 -methyltetrahydrofolic acid, vitamin B12s methylation, 528 Methyl transfer: inversion of configuration, methionine, 115 mechanism, methionine, 113 thiols, methylcobalamin, 312 Methyltransferase enzyme: properties, 135 purification, 135 Methyl(triphenylphosphine)cobaloxime, cobalt-carbon bond, bond leng hs, 505 Microbiological assay, vitamin B12, 7 Microbiological formation, yellow

corrinoids, 228 Migration of group X, electron transfer,

vitamin B12 coenzyme, 555 MO-calculations: aminomutases, 557 corrin:

electrophilic substitution, 212 epimerization, 220 diol dehydrase, 557 ethanolamine ammonia-lyase, 557 methylmalonyl-CoA mutase, 557 vitamin B12 coenzyme, enzymic

reaction, 557 vitamin B12, electrophilic attack, 212 Model for corrin, cobaloximes, 419 Model for ethanolamine ammonia-lyase,

vitamin B12 coenzyme photolysis, 196

Model systems: bis(salicylaldehyde)ethylenediiminecobalt, vitamin B12 coenzyme, 551 cobalt role, 378 diol dehydrase, 532 ligand binding, vitamin B12 coenzyme, 504 mechanism, 383 methylmalonyl-CoA mutase, 532 pKa values, vitamin B12 coenzyme, 504 redox chemistry, vitamin B12 coenzyme,

504 redox potential, vitamin B12 coenzyme,

504 vitamin B12: comparison to, 504 redox chemistry, 513 vitamin B12 coenzyme: alkylcobalt complexes, 551, 564 aminomutases, 571 bis(salicylaldehyde)ethylenediimine-

cobalt(III),551 capped cobaloximes, 533, 565 cobalt-carbon bond cleavage, 551 comparison to, 504 diol dehydrase, 571 enzymic reaction, 501-541, 564-577 ethanolamine ammonia-lyase, 571 glutamate mutase, 570 mechanism, role of, 528 mechanism of action, 543-582 a-methyleneglutarate mutase, 377, 501-541,567

methylmalonyl-CoA mutase, 564 redox chemistry, 513 Modified cobalamins, cobalt-carbon bond

cleavage, 65 Molecular orbitals, bridged cation, 555 pr-Molecular orbitals, corrin, 397 Molecular rearrangements, vitamin B12

coenzyme, 545 Molecular structure in solution, comparison to X-ray structure by nmr spectroscopy, 482 Mono-C-methylated chlorin, structure, 131 Monocarboxylic acid, vitamin B12:

bond angles (tables), 45-53 bond distances (tables), 45-53 cell dimensions, 93 chemical formula, 93

Monocarboxylic acid, vitamin 7 space group, 93 structure, 34

torsion around A-D junction, 57 X-ray crystallographic data, 93 see also Vitamin B12

Monocarboxylic acid (E2), 83 Monoclinic model, vitamin B12r, epr spectroscopy, 439 Monolactone, see Sirolactone Monomethylmercury(II), methylcobalamin, 526 Mutase reactions, vitamin B12 dependent,

table, 328

NADH, cobalamin reduction, 157 NADPH:

methionine biosynthesis, 162 methylcobalamin biosynthesis, 162

Neocobalamins, pK values, steric effects, 489

Neocobinamide, 232, 234. See also Neocorrinoids

Neocobyric acid, total synthesis, 187, 196,232 Neocorrinoids: chromatography, 222 circular dichroism, 222, 225 electronic spectrum, 222 3-epicorrinoids, 224 8-epicorrinoids: biological activity, 225 circular dichroism, 224 13-epicorrinoids, 221 epimerization, 220 optical rotatory dispersion, 222 trifluoroacetic acid, epimerization, 222 see also 3-Epicorrinoids; 8-Epicorrinoids; 13-Epicorrinoids; NeovitaminB12

Neopentylcobalamin: homolytic cleavage, thermolysis, 364 isomerase reactions, 375 rate of decomposition, 368 thermolysis, 552 Neopentyl(pyridine)bis(salicylaldehyde- o-phenylenediimine)cobalt, bond dissociation energy, 512 Neophyl rearrangement, organic radicals, 556 Neovitamin B12: biological activity, 224 bond angles, tables, 45-53 bond distances, tables, 45-53

C-13 epimer, 33 cell dimensions, 93 chemical formula, 93 comparison to vitamin B12, 35 conformations, 209 folding, 60 nmr spectrum, 485 planarity deviations, 61 space group, 93 structure, 34, 224 torsion around A-D junc ion, 57 X-ray crystallographic data, 93 X-ray structure, diagram, 34, 36 see also 13-Epicorrinoids

Nephelauxetic series: electronic spectrum, 409 trans-effect, 336

Neurological abnormalities, pernicious anemia, 2

Neutron diffraction: VitaminB12 coenzyme, 91 vitamin B12 , monocarboxylic acid (E2),

33 Nickel corrin:

bond distances, angles, tables, 45-53 folding, 60

planarity, devia ions, 61 torsion around A-D junction, 57 Nickel 1,19 -dimethyloctadehydrocorrin, catalytic, reduction, 238 Nickel 7,7,12,12,19-pentamethylcorrin: electronic spectrum, 424 magnetic circular dichroism, 424 Nickel(II) 5-cyano-l6-ethoxy-1,8,8,13,13- pentamethyl-14-methylene-CD- secorrin perchlorate: cell dimensions, 96 chemical formula, 96 space group, 96 X-ray diffraction data, 96 Nickel(II) 15 - cy ano -2,2,7,7,12,12- hexamethyl- 1-methylene-AD- secocorrin perchlorate: cell dimensions, 96 chemical formula, 96 space group, 96 X-ray diffraction data, 96 Nickel(II) 15 -cyano -7,7,12,12,19- pentamethylcorrin chloride, conformations, 208 Nickel 15 - cyano -7,7,12,12,19 - pentamethylcorrin: electronic spectrum, 424

Nickel 15-cyano-7,7,12,12,19-pentamcthyl- corrin {Cont'd)

magnetic circular dichroism, 424 Nickel(II)-1,2,2,7,7,12,12-

heptamethyl-15 -cy ano-1,19- epoxysecocorrin perchlorate:

cell dimensions, 97 chemical formula, 97 space group, 97

X-ray diffraction data, 97 Nickel(II) -1,2,2,7,7,1212 -heptamethyl - 15-cyano-18-dehydrocorrin:


X-ray diffraction data, 97 Nickel(II) 1,8,8,13,13 -pentamethyl-5 - cyano -trans-cou'm chloride:

cell dimensions, 95 chemical formula, 95 space group, 95 X-ray crystallographic data, 95

Nico inate mononucleotides: cobalamins, biosynthesis, 153 deamidation, 153

Nitrile hydrolysis, vitamin B12 total synthesis, 191

Nitroalkylcobalamin photolysis, 405 Nitroalkylcobinamide photolysis, 405 Nitroalkylcorrins photolysis, epr

spectrum, 405 Nitromethane:

cobalt alkylation, 280 reaction w ith a quohydroxo Co(III), 336

Nitrosation: corrin, 217 vitamin B12, 217

10-Nitrosocobalamin: electronic spectrum, 217 nomenclature, 17 preparation, 217

Nitrosodurene, reaction with vitamin B12

coenzyme, 298 Nitrosyl chloride, reaction with corrin, 217 Nitrous oxide:

diol dehydrase inhibition, 373 ethanolamine ammonia-lyase inhibition, 373

Nitroxidcs, spin-trapped, 298 Nmr spectroscopy:

biosynthetic studies, 486 cobalamins, isomeric forms, 463-500

cobalt-carbon bond, polarizability, 489

cobalt complexes: cis-effect, 487 trans-effect, 488

cobalt(I) complexes, 486 cobalt(II) complexes, 486 corrin:

cis-effect, 487 trans-effect, 463-500

5,6 -dimethylbenzimidazole: protonation, 494

trans-effect, 488 electronic structure, corrinoids, 487 fluxionality, cobalamins, 490 methylcobalt complexes, bond lengths, 506 methylcorrinoids: 13C containing, 484 trans-effect, 489 molecular structure in solution,

comparison to X-ray structure, 482

nuclear Overhauser effect, 479 pH dependence, cobalamins, 493 structural information, 482 temperature dependence, cobalamins, 490

vitamin B12 biosynthesis, 479 vitamin B12 coenzyme, 465 Nmr spectrum: aquocobalamin, 468 13C, biosynthetic studies: dicyanocobalamin, 112 vitamin B12, 112,480 13 CN-enriched, dicyanocobalamin, 478

C-0 proton, corrin ring, 469 carboxymethylcobalamin, lanthanide

shift reagents, 472 chemical shifts:

vitamin B12,485 vitamin B12 coenzyme, 465

cobalamins, table, 474 cobaloximes, 247 corrin ring, vitamin B12 coenzyme,

469 corriphyrin-3, 135 coupling constants, table, 484 cyanoaquocobinamide, a )3-isomers, 484 5 '-deoxyadenosyl ligand, vitamin B12

coenzyme, 468, 477

vitamin B12r, paramagnetic shifts, 487 vitamin B12s, 486

yellow corrinoids, 229, 485 Noble prize, vitamin B12, 2 Nomenclature, vitamin B12 and derivatives, 17-22 1 -Norbornyl(pyridine)cobaloxime, pre paration, 255 2-Norbornylcobalamin, rate of decomposi tion, 368 Nuclear Overhauser effect: nmr spectroscopy, 479 sirohydrochlorin, octamethyl ester, nmr spectrum, 125 Nucleophilic attack: cobalt-carbon bond cleavage, 527 cobalt(III) complexes, 284 Nucleophilic displacement, R+ from

(alkylcobalt)+,516 Nucleophilicity: bis(salicylaldehyde)ethylenediimine-

cobaltcomplexes, 523 cob(I)aloximes, 523 cob(I)inamide, 250, 251 cobalt(I) complexes, table, 251 definition, 250 diacetylmonoximeimino diacetylmono-

ximatoiminopropane-l,3-cobalt(I), 523

effect of axial ligands, cobalt(I) complexes, 252

vitamin B12s, 251, 523 Nucleoside analogs, vitamin B12 coenzyme, 160 Nucleosides, conformations, table, 70 Nucleoside triphosphates:

adenosylating enzyme, 160 adenosylation, C. tetanomorphum, table,

160 Nucleotide loop:

acid hydrolysis, 234 biosyn hesis:

[R] -l-amino-2-propanol, 149 cobalamins, 148 corrin, 148 glutathione, 152 guanosine diphosphate, 152 Propionibacterium arabinosum,

152 biosynthetic scheme, 149 conformations, 65 reactions, 234-236 Nucleotides, conformations, table, 70

Nmr spectrum (Cont'd) dicyanocobalamin (table), (13C), 476 dicyanocobinamide, table, (13C), 476 5,6-dimethylbenzimidazole, vitamin B12

coenzyme, 468, 477 ethylcobalamin, 468, table, 474 Factor 111,471,472 1 H/ 2H exchange, corrin ring, 469 hydroxocobalamin, 468, table, 474 2-3 '-isopropylidene-5 '-deoxy-0 (D)-

ribosylcobinamidc, 486 isopropyl(tricyclohexylphosphine)

cobaloxime, 506 isopropyl(triphenylphosphine) cobaloxime,

506 lanthanide shift reagents, corrin ring,

471,482 longitudinal relaxation times, vitamin B12,

485 methylcobalamin, 471, table, 474 methylcobaloxime, 490 methylcyanocobalamin, 468 neovitamin B12, 485 nuclear Overhauser effect, siiohydro-

chlorin, oct amethyl e ster, 1 23 paramagnetic sh ifts, cor rin ring, 471 pH, dependence, methylcobalamin,

494 praseodymium:

aquocobalamin, 483 methylcobalamin, 483 vitamin B12,484

vitamin B12 coenzyme, 483 propanolamine, vitamin B12 coenzyme, 467 protonated, vitamin B12 coenzyme, 468 ribosc ring, vitamin B12 coenzyme, 467, 478 side chain, corrin ring, 480 sirolactone, hcptamethyl ester, 123 trimethylated isobacteriochlorins, 132 vinylcobalamin, 490 vitamin B12:

(13C) table, 476 monocarboxylic acid, 471, 486

vitamin B12 coenzyme: 5'-2H-deoxyadenosyl ligand, 471 1HZ2H exchange, 468, 469

protonated, 468 VitaminB12 coenzyme (13 C), table, 476 vitamin B12 coenzyme, table, 474 vitamin B12, table, 474

Numbering, vitamin B12 and derivatives, nomenclature, 18

Octadehydrocorrin, nomenclature, 19 Octamethyl ester: electronic spectrum, sirohydrochlorin, 123

nmr spectrum, nuclear Overhauser effect, sirohydrochlorin, 123

sirolactone, 122 trimethylated isobacteriochlorin electronic spectrum, 132 2,2,7,7,12,13,17,18-Octame hylisobacterio- chlorin: structure, 136 synthesis, 136 Olefin addition: cob(I)aloximes, alkylation, 523 cobalt(I) complexes, alkylation, 523 free radical intermediates, hydridopentacyanocobalt, 518 radical intermediates, hydrido(tri-n- butylphosphine)cobaloxime, 518 Olefin p-complexes: 2-acetoxyalkylcobaloximes, 575 acid catalysis: 2-hydroxyethylcobaloxime, 575 phenacylcobalamin, 575 cob(III)aloxime, 314 cobalt(I) complexes, acrylonitrile, 527 cobalt(III) complexes, 282 1,2-dihydroxyethylcobalt, 574 2,2-dihydroxyethylcobalt, 574 structure, 534 VitaminB12 coenzyme: enzymic role, 534 ethanolamine ammonia-lyase, 575 glutamate mutase, 549, 571, 575 Olefins:

addition to cobalt(I) complexes, mechanism, 256, 262

alkylcorrins, photolysis, 302 cobalt(I) complexes, addition, pH

function, 523 decomposition, alkylcorrins, 365 mechanism: cobaloximes, addition to, 264 cobalt(I) complexes, addition to,

265 hydridocobalt complexes, addition

to, 265 hydridopentacyanocobalt, addition

to, 263

pentacyanocobaltate, reaction with, 276

One-electron oxidation, alkylcobalamins, 515,517

Optically active alkyl ligands, cobaloximes, 268

Optical rotatory dispersion: neocorrinoids, 222 vitamin B12, 223 Orbital energies: corrin, 206, 399 vitamin B12, 206 Orbitals, cobalt(II) complexes, 438, 440 Orbital symmetry, vitamin B12 total

synthesis, 176 Organic radical interaction: epr spectrum: cobalt(II) complexes, 450 enzymic reaction, vitamin B12r, 450 separation, vitamin B121., 452 Organic radical recombination, vitamin B12r rate, 525 Organic radicals: cobalt(II) complexes, reaction with, 271

enzymic reaction, epr spectroscopy, 559

intramolecular 1,2-shifts, 556 neophyl rearrangement, 556 rearrangements, role of cobalt, 531, 533, 556 vitamin B12 coenzyme, enzymic reac tions, 545, 547 vitamin B12f: oxidation, 376 reduc ion, 376 Wagner-Meerwein rearrangement, 556

Organic solvent soluble corrins, 236 Organocobalt complexes:

synthesis, 245-294 see also Alkylcobalamins; Alkyl- cobaloximes; Alkylcorrins; Cobaloximes; Cobalt complexes; Cobalt-carbon bond; Methyl- cobalamin; Vitamin B12 coenzyme

Organolithium reagents, cobalt(III) complexes, alkylation, 517

OrganometalUc chemistry, vitamin B12, 326

Ornithine, 328 Orthoamide, vitamin B12 total synthesis,

178

P. shermanii, isolation sirohydrochlorin, 122

Palladium(II) al kylcobalt complexes, alkylation, 527

Palladium(II) 1 5-cy ano-2,2 ,7,7,12,12- hexamethyl-1-methylene-AD- secocorrin perchlorate, 96

Palladium(II) 1,2 ,2,8,8,12,12-heptamethyl-5-cyano-fraHS-corrin perchlorate, 95

Paper chromatography, corrin, 249 Paramagnetic shifts:

corrin ring, nmr spectrum, 471 nmr spectrum, vitamin B13r, 487 praseodymium, paramagnetic shift reagent, 483

Patterson map, X-ray structure, 97, 98 PBG, see Porphobilinogen Pentacarboxylic acid , ele ctronic spe c-

trum, vitamin B12,417 Pentacyanocobaltate:

alkylation, 502 alkyl halides, re activity tow ards, 521 1,3-diiodopropane, cyclopropane

forma ion, 519 olefins from alkyl halides, 519 reaction with: acetylene, 276 alkyl halides, table, 274 olefins, 276 recombination with radical intermediates, 511 reducing agent, 514 structure, 503 Pentadecaalkylcorrin: circular dichroism, corrin, 237 structure, 237 Pentanal, 4,5-dihydroxypentylcobal-

oxime photolysis, 573 3-Pentylcobalamin, rate of, 371 Periodate oxidation, 2,3-dihydroxy-rc- propylcobalamin, 284 Peripheral amide (corrin): reactions, 230-234 vitamin B12, 230-234 vitamin B12 coenzyme, 41 see also Amide groups, corrin periphery Permanganate oxidation:

corrin, 218, 239 vitamin B12, 218, 239

Pernicious anemia: neurological abnormalities, 2

Outer-sphere electron transfer, Schiff-base complexes, cobalt(II) complexes, 519 Oxidation: alkylcobalamins, one-electron, 517 alkylcobaloximes, hexachloroiridate,

table, 515, 516 carboxylic acids, corrin, 218 chromic acid, corrin, 218 cobalt(III) complexes, carbon monoxide, 515 corrin: meso-methyl groups, 239 permanganate, 218, 219 2,3-dihydroxy-w-propylcobalamin, periodate, 284 dehydrocobinamide, chromic acid, 226 electrochemical, 517 hydrogen peroxide, corrin, 218 methylcobalamin, electrochemical, 517

one-electron, alkylcobaloximes, 515 organic radicals, vitamin B12r, 376 vitamin B12: chromic acid, 218 meso-methyl groups, 239 permanganate, 218, 239 Oxidation state, alkylcobalt complexes,

formal, 514 Oxidative addition, vitamin B12 coenzyme

enzymic reaction, 576 Oxidative cleavage: corrin, 217-220 succinimides, corrin, 217 vitamin B12, succinimides, 217 Oxime hydrolysis, nitrous acid, vitamin B12 total synthesis, 179 O2, alkylcobalamin photolysis, role of, 366 Oxygenated vitamin B121., epr spectrum,

458 Oxygen complex structure, vitamin B12r,

459 Oxygen sensitivity, vitamin B12 coenzyme,

551 Ozonolysis:

corrin, 218 heptamethyl cobyrinic acid, 115 heptamethyl dicyano( 10-bromocobyri-

nate), 218 secocorrindione, corrin, 219 vitamin B12 , total synthesis, 174, 218

X-ray crystallographic data, vitamin B12, 94

X-ray structure, diagram, vitamin B12, 34

see also Vitamin B12

Phosphocellulose, corrin chromatography, 249 5-Phosphoribosyl-l-pyrophosphate,

cobalamins biosynthesis, 153 Phosphorylation, [R]-l-amino-2-

propanol, 151 Photoaquation: alkylcorrins, 301 cobalt-carbon bond, 362 cobalt(III) complexes, 296 corrin, 330 Photochemical path, vitamin B12: ring closure, 196 total synthesis, 169-200 Photochemistry: cobalt-carbon bond: cleavage, 362 dissociation energy determination, 507 secocorrins, metallo, 209 a.b, Photoisomerization, methylcorrinoids, 301 Photolability: alkylcobalamins, base-on, off, 303, 524 alkylcobalt complexes, 55 3 Photolysis: acetaldehyde: ethanolamine and vitamin B12 coenzyme 298

ethylene glycol and vitamin B12 coen zyme, 298 alkylcobalamins, quantum yield, 300- 303 alkylcobaloximes, 300-303, 364 alkylcobalt complexes, 524, 552 anaerobic, alkylcobalt complexes, 553 aristeromycyclocobalamin, 297 bis(acetylacetone)ethylenediimine-

cobalt, alkyl complexes, 524 bis(salicylaldehyde)ethylenediimine-

cobalt(III): methyl complex, 301 propyl complex, 302 bis(salicylaldehyde)ethylenediimine-

cobalt complexes, alkyl complexes, 524

carboxylatopentaaminecobalt(III) complexes, 272

carboxymethylcobalamin, 302

Pernicious anemia (Cont'd) vitamin B12, 1

PH: cobalt-free corrin, electronic spectrum,

401 decomposition rates:

alkylcobinamides, 370 isopropylcobalamin, 370

dependence: cobalamins, nmr spectroscopy, 493

methylcobalamin, nmr spectrum, 494 descobaltocobamide, electronic spectrum, 211 function, olefins, cobalt(I) complexes, 523

Phenacylcobalamin, olefin p-complexes, acid catalysis, 575

Phenolatocobalamin, electronic spectrum, 404

Phenol extraction, corrin, 249 Phenylacetonitrile, aquocobalamin reac-

tion with, 279 Phenylacetylene, addition to cobalt(I)

complexes, 256 a-Phenylethylamine, resolving agent, vita-

min B12 total synthesis, 183 1 -Phenylethylcobaloximes:

axial ligands role, activation enthalpy, 511

cob(II)aloximes, reaction with, 504 thermolysis, 304 1-Phenylethyl(pyridine)cobaloxime: bond dissociation energy, axial ligands, role, 510 equilibrium determination, 508 cobalt-carbon bond, thermal dis sociation,- 509 Phenyl(pyridine)cobaloxime, preparation, Grignard reagent, 271, 278 Phenylthiomethyl chloride, reaction with corrin, 214 5'-Phosphate: bond angles, tables, vitamin B12, 45- 53

bond distances, tables, vitamin B12, 45-53

cell dimensions, vitamin B12 , 94 chemical formula, vitamin B12, 94 planarity deviations, vitamin B12, 61 space group, vitamin B12, 94 structure, vitamin B12, 34 torsion around A-D junction, vitamin B12, 57

1,4,8,11-tetraazacyclotetradecane, alkyl complexes, 524

trichloromethylcobalamin, 303 vitamin B12, 404 vitamin B12 coenzyme, 296, 363 vitamin B12r, methylcobalamin, 300 vitamin B12s: acetone, 302 alkylcobalamins, 302 Photoreduction, cobalt(III) complexes, 296 Pinacoylcobalamin, 371 5,6-dimethylbenzimidazole, 351 pK values: alkylcobalamins, 494

benzimidazole, table, alkylcobalamins, 54, 351

benzimidazole, vitamin B12 coenzyme, 351

bis(acetylacetone)ethylenediiminecobalt, 504

bis(salicylaldehyde-o-phenylenediimine) cobalt, 504

7,7'(CH3 )2 bis(salicylaldehyde)ethylenediiminecobalt, 504

carboxymethylcobalamin, 316 cobalt, hydrides, 335 corrin, raeso-methyl groups, 239 diacetylmonoximeimino diacetylmono-

ximatoiminopropane-1,3-cobalt, 504

hydridocobalamin, 506 hydridopentacyanocobalt, 506 hydrido(tri-H-butylphosphine) cobaloxime, 506 steric effects, neocobalamins, 489 vitamin B12 coenzyme, model systems, 504

vitamin B12 , meso-me hyl groups, 234 vitamin B128, 364 Planarity: cobaloximes, 505 cobalt corrins, 54, 61, 208 Platinum(IV) alkylcobalt complexes, alkylation, 527 Pleochroism, vitamin B12 crystal morpho logy, 25 Polarizability, nmr spectroscopy cobalt- c arbon bond,489 Polarization effects: corrin, electronic spectrum, 402 vitamin B12, 402 Porphobilinogen, incorporation into corrin, 111

Photolysis (Cont'd) chloromethylcobalamin, 303 cobaloximes, 419 cobalt-carbon bond, vitamin Bj2s, 296 5'-deoxyadenosine, vitamin B12 coenzyme

and thiols, 299 diacetylmonoximeimino diacetylmono-

ximatoiminopropane-l,3-cobalt(I), alkyl complexes, 524

dichloromethylcobalamine, 303 4,5-dihydroxypentylcobaloxime, 534 dihydroxypropylcobalamin:

glyceraldehyde, 302 glyceric acid, 302 glycerol, 302

electronic spectrum, vitamin B12 coenzyme, 296

epr spectroscopy, alkylcobaloximes, 525 epr spectrum, nitroalkylcorrins, 405 ethane, methylcobalamin, 300 ethylcobalamin, 302 frozen solution, epr, vitamin B12 coen-

zyme, 299 3-hydroxyisopropyl(pyridine) cobaloxime,

302 2' ,3' ,0-isopropylidene-5 '-deoxy uridyl-

cobalamin, 297 methylcobalamin, 300, 362, 404 methylcobaloxime, cob(II)aloximes, 301 methylperoxocobaloxime, methylcobalo-

xime, 553 methyl radicals, methylcobalamin, 300 model for eth anolamine ammonia ly ase,

vitamin B12 coenzyme, 298 nitroalkylcobalamin, 405 nitroalkylcobinamide, 405 olefins, alkylcorrins, 302 pentanal, 4,5-dihydroxypentylcobalo-

xime, 573 in presence of nitrosodurene, vitamin

B12 coenzyme, 298 in presen ce of thiols, v itamin B 12 coen-

zyme, 298 propylcobalamin, 302 propylcobaloxime, 302 quantum yield:

alkylcobaloximes, 525 alkylcobalt complexes, 55 3 vitamin B12 coenzyme, 303

radical traps, alkylcobalt complexes, 553

role of O2, alkylcobalamins, 366 spin-traps, alkylcobalt complexes, 553

hydridocobalamin, secondary alkylcorrinoids, 253,365,552

hydrido(tri-w-butylphosphine)cobaloxime, 253

b-hydroxy-n-propyl(pyridine)coboloxime, 257 4-hydroxy-2,2,6,6-tetramethylpiperidine-

N-oxylcobamide coenzyme, 267 lactones (corrin ring), 226 methyl(aquo)cobyrinic hepta tert-

alcohol, 278 l-methyl-2,2-diphenylcyclopropyl

(pyridine)cobaloxime, 254 N-methyleneaniline(pyridine)cobalo-

xime, 258 10-nitrosocobalamin, 217 l-norbornyl(pyridine)cobaloxime, 255 phenyl(pyridine)cobaloxime, 271 pulse radiolysis, a-hydroxyalkylcobalt

complexes, 273 reactions, 2-hydroxyalkylcobaloximes, 284 rhodium cobyrinic acid-c,c-diamide, 37 sirohydrochlorin, 257 p-trifluoromethylphenyl(pyridne) cobalo-

xine, 271 vinylcobaloxime, 261 vinylcobalt porphyrins, diazoalkanes, 280 vitamin B12 coenzyme analogs, 5'-deoxy-

5'-halonucleosides, 267 vitamin B12: carboxylic acids, 231

yellow corrinoids, 215, 228-230 vitamin B12r, 439

yellow corrinoids, gCoPSE, 40 Preuro'gen, 118

Principal axes, vitamin B12r epr spectroscopy, 439

Prokaryotes: cobalt-carbon bond biosynthesis,

155- 163 vitamin B12 coenzyme biosynthesis,

156- 161 Propane-1,2- diol , see Propylene gly col [I-2H2 ]Propane-l,2-diol, vitamin B12

coenzyme kinetic isotope effect, 554

Propanolamine, v itamin B12 coenzy me nmr spectrum, 465, 470

Propargyl alcoho l, addition to cobalt(I) complexes, 256

Propionaldehyde, 328 Propionamide side chain, vitamin B12 , 30

Porphobilinogen deaminase: corrin biosynthesis, 139 deamination, aminomethylbilanes, 118

[8-13C] Porphobilinogen, vitamin B12 biosynthesis, 480

Potassium reduction, cobalt complexes, 254 Powder samples, vitamin B12r epr spectro-

scopy, 439 Praseodymium corrin shift reagent, table,

483 Preferred coordination number, cobalt complexes, 504 Preparation: acetoxyalkylcobaloximes, 284 1-adamantyl(pyridine)cobaloxime, 255 8-aminocobyrinic acid abcdefg-hexamethyl

ester c-lactam, 236 8-aminoethylcobalt complexes, 2§7 benzoyl(l-pyridino)methanide(chloro)

cobaloxime, 276 10-bromocobalamin, 216 b-carbomethoxyphenylcobinamide, 271 15-carboxy-15-norcobinamide, 239 10-chlorodehydrovitamin B12, 215 Coa-cyano-Cob-alkylcobamides, 307 cobalt(III) complexes, cobalt-carbon

bond, 271-277 cobyrininic acid-tf,c-diamide, 37 corrin, organic solvent soluble, 236 cyclohexyl-3,5,6-trimethylbenzimi-

dazoylcobamide, 255 dansylamidopropylcobalamin, 267 5 '-deoxy( 1 ,N6 -etheno)-adenosylco-

balamin, 285 2,6-diaminonebutavinylcobalamin, 267 5,15-dicarboxy-5,15-dinorcobinamide,

239 dicobaloximes, 268 2.2- diethoxyethylcobalamin, 28 1 dihydroxyalkylcobaloximes, 284 1.2- dioxa-2-cyclopentylmethylcobalo-

xime, 282 l,N6-ethenoadenosylcobalamin, 267 formycinylcobalamin, 267 formylmethylcobalamin, 283, 315 formylmethylcobaloxime, 315 Grignard reagent, phenyl(pyridine)cobalo-

xime, 278 halomethylcobalt porphyrins, diazo-

methane, 280 heptamethyl dicyano-5, 15-bisnorco-

byrinate, 239 heptametyl dicyanocobyrinate, 236

Protoporphyrin IX, structure, 110 Prototrophs, cobalamins, 155 Puckering, corrin ring, 54 Pulse radiolysis:

acetaldehyde, ethylene glycol, 574 aquocobalamin, 318 Me[14] -diene N4, 574 1,2-dihydroxyethyl radical, 574 a-hydroxyalkylcobalt complexes,

preparation, 273 vitamin B12, 318 vitamin B12 coenzyme, 318

vitamin B12r-, 318 Purification, methyltransferase enzyme, 135 Purine nuleosides, vtamin B12 coenyme,

300 Pyrazolopyrimidine nucleosidylcobalamin,

reac ion with cyanide, 307 Pyridinatocobalamin, electronic spectrum,

411 Pyridine complexes, hydrolysis, alkyl- cobalaoximes, 248 Pyridoxal phosphate: aminomutases, 329 cofactor, 2,6-diaminohexanoate mutase, 574 Pyrolysis: cobalt-carbon bond, 303 vitamin B12, 239

14N-Quadrupole interaction, vitamin B 12r, 441

Quantum yield: alkylcobaloximes, photolysis, 524 alkylcobalt complexes, photolysis, 553 photolysis, alkylcobalamins, 303 vitamin B12 coenzyme, photolysis, 303

Racemization, X-ray crystallography, R-a-cyanoethyl(S-a-methylbenzylamine)cobaloxime, 88

Radical cations, vitamin B12 coenzyme, ethanolamine ammonia-lyase, 573

Radical doublet intermediates: enzymic reaction epr spectroscopy, 450

vitamin B12 coenzyme enzymic reaction, 450 Radical intermediates: aminomutases, 556

Propionibacterium arabinosum, nucleotide loop biosynthesis, 152

Propionibacterium shermanii: corrin, biosynthesis, 112 source of corrin, 146 Proposed mechanisms, isomerase reactions, 383 Propylaquocobaloxime, redox potential, 516 Propylbis(acetylacetone)ethylenediimine-

cobalt, radical scav engers, therm aldecomposition, 512

Propyibis(salicylaldehyde)ethy Iene- diiminecobalt, radical scavengers, thermal decomposition, 512

Propylbis(Salicylaldehyde)-O -phenylene-diiminecobalt, ra dical scavengers, thermal decomposition, 512

Propylcobalamin, photolysis, 302 Propylcobaloxime, photolysis, 302 n - Propylcyanocobalamin, electronic

spectrum, 413 Propylene glycol, 328 Propyl(pyridine)bis(salicylaldehyde-o-

phenylenediimine)cobalt, bond dissociation energy, 512

Propyne, addition to cobalt(I) complexes, 256

Prosthetic group sulfite reductase, siroheme, 128

Protection by peripheral groups, cobalt-carbon bond, 90

Protection by side chains, vitamin Bu

coenzyme cobalt-carbon bond, 41 Protein:

cobalt-carbon bond, labilization, 333 distortion, vitamin B12 coenzyme, 373

vitamin B12 coenzyme: enzymic reaction, 555 role of, 329 Protein effects, cobalt-carbon bond angles, 373 Protonated: nmr spectrum, vitamin B12 coenzyme, 466 radical intermediates, 557 Protonation: alkylcobalamins, 351 nmr spectroscopy, 5,6-dimethyl-

benzimidazole, 494 vitamin B12 coenzyme, 351 vitamin B12s, 364

Radical intermediates (Cont'd) bis(salicylaldehyde-o-phenylene-

diimine)cobalt(II), alkylation, 518

cobalt(II) complexes, alkylation, 518

diol dehydrase, 556 enzymic reaction, 2-amino-l-propanol,

450 ethanolamine ammonia-lyase, 556 glutamate mutase, 556 hydrido(tri-n-butylphosphine)-

cobaloxime, olefin addition, 518

a-methyleneglutarate mutase, 557 pentacyanocobaltate, recombination

with, 511 protonated, 557 vitamin B12r alkylation, 520 Radical pair recombination, CIDNP

measurements, 512 Radical reactions, vitamin B12, yellow

corrinoids, 229 Radical rearrangements: aminoalcohols (vicinal), 573 1,2-diols, 573 Radical recombination: corrin, 363 vitamin Blsr, 363 Radical scavengers, alkylcobalt complexes, 301, 512 Radical transfer, cobalt-carbon bond

cleavage, 526 Radical traps, alkylcobalt complexes,

photolysis, 553 Rapid reaction intermediate: epr spectrum: epr spectroscopy, 455 ribonucleotide reductase, 455 ethanolamine ammonia-lyase, 455 vitamin B12 coenzyme, enzymic reaction, 455 Rate of: acid catalyzed decomposition: 2-butylcobalamin, 371 isopropylcobalamin, 371 decomposition: alkylcobalamins, very strained, 365,

368, table, 371 cyclobutylcobalamin, 368 cyclohexylcobalamin, 368 cyclopentylcobalamin, 368 cyclopropylcobalamin, 368

methylcobalamin, 368 neopentylcobalamin, 368 2- norbornylcobalamin, 368

2- methyl-2-butylcobalamin, 371 organic radical recombination, vitamin

B12r-, 525 3- pentylcobalamin, 371 pinacoylcobalamin, 371

Rates, alkylcobaloxime axial ligand exchange, 248

Rates of hydrolysis, steric, amide groups (corrin periphery), 231

Ratio, methylcobalamin, vitamin B12

coenzyme, 161 Reaction pathways: diol dehydrase, 555, 558 ethanolamine ammonia-lyase, 555 olefin p-complexes: aminomutases, 573 diol dehydrase, 575 vitamin B12 coenzyme: enzymic reaction, 555 ethanolamine ammonia-lyase, 573 glutamate mutase, 571 a-methyleneglutarate mutase, 570 methylmalonyl-CoA mutase, 565, 566 Reactions: alkyl ugands, 295-323 cobalt(I) complexes, 263 5 '-deoxyadenosyl radical, formation, 297, 363

2-hydroxyalkylcobaloximes, preparation, 284

methyl radicals, 300 nucleotide loop, 234-236 peripheral amide groups (corrin), 230-234 vitamin B12, chloramine T, 215 Reaction with: acetylene, pentacyanocobaltate, 276 acid:

alkylcobalamins, 313 l,3-dioxo-2-cyclopentylmethylcobala-

min, 315 formylmethylcobalamin, 314 hydroxyalkylcobaloximes, 313 4-hydroxy-n-butylcobaloxime, 314 3- hydroxy-n-propylcobaloxime, 314 (3-hydroxy-H -propylpyridinato-

cobaloxime, 314 methyl(aquo)cobaloxime, 313 vinylcobalamin, 314 alkali:

adenosylcobaloxime, 307

alkylcobalamins, 306 aristeromycyclocobalamin, 306 N-benzoyladenosylcobalamin, 306 Coa-adenyl-Co(3-adenosylcobalamin, 305 Coa-aquo-Co(Jadenosylcobamide, 306 Coa-aquo-Co(3-adenosyl(3,5,6-trimethyl-

benzimidazolecobamide), 306 difluorochloromethylcobalamin, 307 formycyclobalamin, 307 pyrazolopyrimidine nueleosidylcobala-

min, 307 N-tosylcytidylcobalamin, 306 triethylaminoethylcobalamin, 307 trifluoromethylcobalamin, 307 vitamin B12 coenzyme, 305

a,b-dibromoe hyl acetate, vitamin B12

coenzyme, 285 electrophiles, cobalt-carbon bond, 312-317 equilibrium data, cob(II)aloximes, 504 hydrogen cyanide, vitamin B12 coenzyme,

306 hydroxide:

aristeromycylcobalamin, 307 cob(I)aloxime, trifluoromethyl-

cobaloxime, 309 b-hydroxyisopropylcobaloxime, 310 b-hydroxy-n-propylcobaloxime, 310

hydroxylamine: acetylcobalamin, 312 acetylglycobalamin, 312 glyglycobalamin, 312

iodine, vitamin B12 , 226 kinetics:

cob(II)aloximes, 504 cobalt(II) complexes, 273 table, cobalt(II) complexes, 274

malononitrile, aquocobalamin, 279 mercaptides:

alkylcobaloximes, 311 methyl(aquo)cobaloxime, 311

metal ions, cobalamins, 495 methylmagnesium iodide, heptamethylcobyrinate, 278 methylmercaptide, methylcobalamin, 311 olefins, pentacyanocobaltate, 276 organic radicals, cobalt(II) complexes, 271 phenylacetonitrile, aquocobalamin, 279 1 -phenylethylcobaloximes, cob(Il)alo-

ximes, 504 styrene and hydrogen, cob(II)aloximes,

504

Reaction with (Cont'd) cob(I)aloxime, 2-hydroxycthylco- baloxime, 310 cyanocthylcobalamin, 310 dihalomethylcobaloximes, 309 halomethylcobaloximes, 308 (3-hydroxyalkylcobaloximcs, 310 trans-2-hydroxy cyclohexy lcobaloxime, 311 hydroxycthylcobalamin, 311 hydroxyethylcobinamide, 311 me hoxycarbonylethylcobalamin, 310 trimethylaminoethylcobalamin, 310 vitamin B12 coenzyme, 307

alkyl halides, cobalt(II) complexes, 273 alkyl halides, table:

pentacyanocobaltate, 274 vitamin B12r, 274

aquohydroxo Co(III): acetone, 336 nitromcthane, 336

aiyl halides, vitamin B12 s, 271 ascorbic acid, vitamin B12, 229 carbanions:

bissalicylaldehyde)ethylenediimine- eobalt(III), 279

cobalt(III) complexes, 279 cob(I)aloxime, 1,1 ,bis-(p-chlorophenyl)-

2,2,2-tiichloioethane, 266 cobalt(I) complexes:

threo-3,3-dimethylbutyl-l ,2-d2 -trifluoromethyl sulfonate, 260

epoxides, 256 etheneimine, 257

cobalt(III) complexes: carbenes, 279 enols, 279

ethyl vinyl ether, 281 2-hydroxyethyl vinyl ether, 282 malononitrile, 279 cobinamide guanosine diphosphate, 5,6-dimethylbenzimidazole-5- nucleotide, 153 corrin: chloramine T, 215

dimethyl(methylene)ammonium iodide, 213

hydratcd electrons, 318 nitrosyl chloride, 217 phenylthiomethyl chloride, 214 cyanide: ara-adenosylcobalamin, 306 L-adenosylcobalamin, 306

vitamin B12r methyl radicals, 553 Redox chemistry:

alkylcobaloximes, 515 cobalt, unique biologically, 340 diacetylmonoximeimino diacetyl-

monoximatoiminopropane-1,3- cobalt, alkyl complexes, 514

model systems: vitamin B12,513 vitamin B12 coenzyme, 513

Schiff-base complexes, Cobalt complexes, 514

vitamin B 12 coe nzyme, model sy stems,504Redox potential:

alkylcobaloximes, table, 516 aquocobalamin, 514 benzylaquocobaloxime, 516 bis (acetylacetone)ethy lenediimine-

cobalt, bis(salicylaldehyde)- ethylenediiminecobalt, 504

bis (salicylaldehyde-o-phenylenediimine)- cobalt, 504

cobalt(I) complexes, electron-donor strength, ligand, 251, 504

diacetylmonoximeimino diacetylmonoximatoiminopropane-1,3- cobalt, 504

isopropylaquocobaloxime, 516 methyl(aquo)cobaloxime, 516 propylaquocobaloxime, 516 vitamin B12 coenzyme, model systems,

504 Reduced forms, sirohydrochlorin, 123 Reduction: acetic acid, carbon dioxide, 528 aquocobalamin, enzymic, 157 chromium(II), cobalt complexes, 254 cobalt complexes:

hydrogen,252 potassium, 254 sodium, 254 sodium amalgam, 254

sodium borohydride, 251 diaquocobinamide, formate, 447 electrochemistry, cobalt complexes, 254 FAD, cobalamins, 157 FMN, cobalamins, 157 LiAlH4, heptamethyl dicyanocobyrinate 237 mcthylcobalamin, carbon dioxide, 528 NADH, cobalamins, 157 nickel 1,19-dimethyloctadehydrocorrin,

catalytic, 238

Reaction with (Cont'd) tetracy anoethylene: alkylcobalt complexes, 285 cinnamyl(imidazole)cobaloxime, 286 trifluoroacetic acid, vitamin B12 , 223 vinyl ethers, cobalt(III) complexes, 281 vitamin B12 coenzyme, nitrosodurene,

298 vitamin Bnr: benzyl bromide, 513 5 '-deoxyadenosyl radical, 373 vitamin B12s: benzyl bromide, 513 cyclodecyl-l-d-iodide, 261 dimethylbromome hyl)malonate, 564 Reactivity toward: alkyl halides, table cobalt(II) complexes, 521

bis (salicylaldehyde-o -phenylenediimine)- cobalt(II)(py), alkyl halides, 521

pentacyanocobaltate, alkyl halides, 521 triphenylphosphine cob(II)aloximes,

alkyl halides, 521 vitamin B12r, alkyl halides, 521 Rearrangements: but-3-enylcobalamin, cyclopropyl-

carbinylcobalamin, 567 but-3-enyl(pyridine)cobaloxime, cyclo-

propylcarbinyl(pyridine)- cobaloxime, 568

but-3-enyl radical, cyclopropylcarbinyl radical, 557

cyclopropylcarbinylcobalamin, 379 cyclopropylcarbinylcobaloximes, 381 cyclopropylcarbinyl radical, 557 1,2-dihydroxyethyl radical, 532 kinetics, cyclopropylcarbinyl radical,

567 1-methyl-6«r-3-enyl(pyridinc)cobaloxime,

3-methyleyclopropy lcarbinyl- (pyridine)cobaloxime, 569

2-methyl-6ur-3-enyl(pyridine)cobaloxime, 1-methyl-tor -3-cnyl(pyridine)- cobaloxime, 569 organic radicals, 531, 556 role of cobalt, organic radicals, 533 Recombination: alkyl radicals, cobalt, 335 CIDNP measurements, radical pairs, 512 cob(II)alamin, methyl radicals, 511 Cobalt(II) complexes, methyl radicals, 335 radical intermediates, pentacyanocobaltate, 511

comparison to, cobalt complexes, 72 folding, 60 planarity deviations, 61 structure, 34 torsion around A-D junc ion, 57

X-ray crystallographic data, 72 Rhodium dicyano[cobyrinic acid-a-c- diamide]:


X-ray diffraction data, 94 b-Ribazole, vitamin B12 total synthesis, 198 Ribonucleotide reductase:

affinity chromatography, 268 5'-deoxyadenosine, vitamin B12

coenzyme, 577 5-deoxyadenosyl radical, vitamin B,2

coenzyme, 577 epr spectroscopy, enzymic reaction,

558 epr spectrum, enzymic reaction, 451 from Escherichia coli, 545 hydrogen exchange, with solvent, 449 rapid reaction intermediate, epr spectrum, 455 thiyl radical, vitamin B12 coenzyme, 577 vitamin B12 coenzyme, enzymic reaction, 529 vitamin B12r formation, Lactobacillus

leichmanni, 439 vitamin B12r: binding to, 442 reduction of vitamin B12,434 D-Ribose, vitamin B12 total synthesis, 198 Ribose-l-phosphate, cobalamins biosyn thesis, 153 Ribose ring: conformation, vitamin B12 coenzyme, 550 554

nmr spectrum(13 C), 478 vitamin B12 coenzyme, nmr spectrum, 465, 470

Ring C, vitamin B12 total synthesis, (+) camphor, 184 Ring closure, 190, 196 photochemical, secocorrins, 196 vitamin B12, total synthesis, 197 Ring puckering, vitamin B12 coenzyme, 41 Rings A -D, vitamin B 12 total synthesis, 197 Rings B-C1 vitamin B12 total synthesis, 197

Reduction (Cont'd) organic radicals, vitamin Bnr, 376 sirohydrochlorin, sirolactone, 122 sodium borohydride: cobaloximes, 251 cobalt complexes, 251 thiols, cobalt complexes, 254 zinc/acetic acid, vitamin B12a, 365 Reduction of vitamin B12, ribonucleotide

reductase, vitamin B12r, 434 Reduction to heptaol, heptamethyl dicyano-

cobyrinate, 226 Reductive alkylation: cobaloximes, 248

cobalt complexes, mechanism, 250, 258- 267

Reductive arylation, electron transfer, mechanism, 3 cobalt complexes, 271

Reductive cleavage: alkylcobalamins, vitamin B121., 317 carbon monoxide, cobalt-carbon bond, 515

cobalt-carbon bond, 317 methylcobalamin, H2/Pt, 317 thiols, cobalt-carbon bond, 515 Refractive index, vitamin B12 crystal morphology, 25 Regiospecific aldol, vitamin B12 total

synthesis, 179 Resonance Raman spectrum, corrin, 398 Retro-Claisen, vitamin B12 total synthesis,

174 Reversibility: b-elimination, 367


R factor, X-ray structure, 97 R+ from (alkylcobalt)+, crystallography, R-a -cyanoethyl(S-a -methylbenzylamine)cobaloxime, 88 Rhodium: incorpora ion into: 15-cyano-l,2,7,7,12,12-hyptamethyl-

corrin, 211 vitamin B12, 211 Rhodium analog, vitamin B12,211 Rhodium cobyrinic acid-a,c-diamide: preparation, 37 X-ray structure, diagram, 34 Rhodium corrin: bond angles, tables, 45-53 bond distances, tables, 45-53

Selenocyanocobalamin, 93 Sephadex corrin chromatography, 249 Shift reagent, corrin ring, gadolinium(III),

472,482 Side chain: amide, vitamin B12, hydrolysis, 33 conformations: corrin, 208 corrin ring, 52, 54, 63 table, 52, 54 vitamin B12, 208 corrin, 63

corrin ring, nmr spectrum(13 C), 480 disorder, vitamin B12 monocarboxylic

acid (E2) X-ray structure, diagram, 34

modification, binding to apoenzyme, 65 vitamin B12 : acetamide, 30 propionamide, 30 vitamin B12 coenzyme, cobalt-carbon bond, protection, 41 Sign inversion, circular dichroism, corrin, 422 Simulation: azidocob(II)inamide, epr spectrum, 445 cob(II)amides, epr spectrum, 446 histidine cob(II)amide, epr spectrum, 445

Single crystals, vitamin B12r epr spec troscopy, 439 Siroheme: demetallation, 128 prosthetic group, sulfite reductase, 128 Sirohydrochlorin:

biosynthesis, 126 bislactone, 122 circular dichroism, 122 conversion to, sirolactone, 126 incorporation into:

C tetanomorphum, 126 cobyrinic acid, 126

interconversion, sirolactone, 123 isolation, desulfoviridin, 122 monolactone, 122 octamethyl ester:

electronic spectrum, 125 nmr spectrum, nuclear Overhauser effect, 130 P. shermanii, isolation, 122 preparation, 257 reduced forms, 135

Ring structure, yellow corrinoids, 37 Role in formation of yellow corrinoids,

ascorbic acid, 39 Role in vitamin B12 chemistry, cobalt, 333,

335 Role of:

cobalt, organic radicals, rearrangements, 533

cobalt-carbon intermediate, carbon- skeleton rearrangements, 382

4s and 4p orbitals, cobalt-carbon bond, 338

model systems, vitamin B12 coenzyme, mechanism, 528

O2, alkylcobalamin photolysis, 366 protein, vitamin B12 coenzyme, 329

7,7'(CH3)2 SALEN, structure, 503 Scavenger, vitamin B12r, methyl radicals, 300 Schiff-basc complexes:

acidity, 506 alkylcobalt complexes, bond dissociation

energy, 512 alkylcobalt(IV) complexes, 516 cobalt complexes, redox chemistry, 514 cobalt(lll) complexes, outer sphere electron transfer, 519 Secocorrindione: corrin ozonolysis, 219 cyclization, corrin, 220 structure, 219 Secocorrins: bond angles, distances, tables, 45-53 Intermediates in corrin biosynthesis, 116

metal complexes, X-ray diffraction data, 96

metallo, photochemistry, 209 ring closure, photochemical, 196 structure, 78, 116 torsion around A-D junction, 57 total synthesis, 196

X-ray crystallographic data, metal complexes, 77 Secondary alkylcobalamins, 255 Secondary alkylcorrinoids, preparation,

hydridocobalamin, 552 Sclenocyanatocobalamin, electronic

spectrum, 411 Selenocyanide:

selenium location, vitamin B12, 27 X-ray diffraction data, vitamin B12, 26

Spiro lactones (corrin ring), 226 Stability:

benzylcobalamin, 255 benzylcobalt(octaethylporphyrin),

255 cobalt, hydrides, 335 cobalt-carbon bond, vitamin B12

coenzyme, 330, 335, 366 Stabilization: 5-deoxyadenosyl carbocation, 549 5'-deoxyadenosyl radical, 548 Stable 5-coordinate cobalt(III) complexes, 506 Stable yellow corrinoids, see Yellow corrinoids Standard electronic spectrum, vitamin B12, conversion to dicyanocobalamin, 395 Stereochemistry: alkylcobalt complexes, mercury(II), 526

alkynes, addition to, 256 cob(I)aloximes, alkylation, 523 cobalt-carbon bond, halogen

cleavage, 316 cobalt(I) complexes, alkylation,

523 methionine, methylation, 113 (S)-methylheptylpyridinatocobal-

oxime, iodine cleavage, 317 vinyl halides, alkylation, cobalt(I)

complexes, 260 vitamin B12s, alkylation, 260, 523 Stereospecific thermal cyclization,

vitamin B12 total syn hesis, 176

Steric compression: distortion cobalt-carbon bond, 359 X-ray structure, vitamin B12 coenzyme, 359 Steric crowding: bond length, cobalt-carbon bond, 505

cobalt-carbon bond strengths, 506 vitamin B12,506 vitamin B12 coenzyme, 506

Steric distortion, effects, 367 Steric effects:

bond dissociation energy, cobalt- carbon bond,512

cobaloximes, 86 cobalt-carbon bond, bond dis-

sociation energy, 531

Sirohydrochlorin (Cont'd) sirolactone reduction, 122 structure, 122-124

Sirolactone: from P. shermanii, 123 heptamethyl ester, nmr spectrum,

125 octamethyl ester, 122 reduction, sirohydrochlorin, 122 sirohydrochlorin: conversion to, 123 interconversion, 123 structure, 123, 124 see also Corriphyrin-4, structure Sodium amalgam reduction, cobalt complexes, 254 Sodium borohydride: cobaloximes, reduction, 251 cobalt complexes: catalysis, 252 reduction, 251 reduction, cobalt complexes, 251 Sodium reduction, cobalt complexes, 254 Solu ion thermolysis, ethylcobalamin,

304 Solvent effects: electronic spectrum: vitamin B12 , 409, 410 vitamin B12 coenzyme, 410 Space groups, corrin derivatives, 93- 97 Spectrochemical series, rnzns-effect,

336 Spin-forbidden transitions, electronic

spectrum, 406 Spin-Hamiltonian:

cobalt(II) complexes, 436 vitamin B12 r , 441

Spin-labelled analogs, vitamin B12

coenzyme, 267 Spin-lattice relaxation times:

carboxymethylcobalamin, 492 ethylcobalamin, 492 hydroxyethylcobalamin, 492 methylcobalamin, 492 vitamin B12 coenzyme, 492

Spin-trapped nitroxides, 2 98 Spin-traps, alkylcobalt complex

photolysis, 553 Spirocyclic intermediate:

corrin biosynthesis, 118 structure, 119

Steric effcets (Cont'd) cobalt-carbon bond angles, 355, 372 ligand equilibria, vitamin B12 co-

enzyme, 341 ligand exchange, alkylcobalamins,

341 neocobalamins, pK values, 489 origin, corrin, 355 on structure, alkylcobalamins, 341 transmission, corrin, 355 Steric interactions: cobalt-carbon bond, labilization by, 361 with corrin ring, epr spectrum, 5,6-dimethylbenzimida zole, 448 epr spectrum: cobinamides, 448 vitamin B12r, 442, 448 Steric requirements, corrin, axial

ligands, 255 Strain orbital: corrin, 400, 411

vitamin B12 coenzyme, 411, 560 Streptomyces griseus, methylcobala-

min biosynthesis, 161 Structural comparison to vitamin B12,

vitamin B12 coenzyme, 41 Structural information, nmr spectro scopy,- 482 Structure: adenosine-5'-carboxaldehyde, 297 aminomethylbilane, 118 aquocyanocobyric acid, 205 bis(acetylacetone)ethylenediimine-

cobalt(IIl), 503 bis(salicylaldehyde)ethylenediimine-

cobalt, 557 bis(salicylaldehyde)ethylenediimine-

cobalt(III), 503,552 bis(salicylaldehyde-o-phenylene-

diiminecobalt(III), 503 bridged cobaloximes, 87, 269 capped cobaloximes, 533, 565 cobalocorrin, 203 cobaloxime, 246 cobalt 15-cyano-2,2,7,7,12,12-

hexamethylcorrin, 424 cobalt 15-cyano-7,7,12,12-tetra-

methylcorrin, 424 cobalt 2,2,7,7,12,12,15-hepta-

methylcorrin, 424

cobalt 2,2,7,7,12,12-hexamethylcorrin, 424

cobalt 7,7,12,12-tetramethylcorrin, 424

cobinamides, 235 cobyric acid, 34, 148, 170 cobyrinic acid, 109 corriphyrin-3, 134 corriphyrin-4, 124 corrole, 203 15-cyano-l,2,2,7,7,12,12-hepta-

methylcorrin, 211 cyclic nucleoside, 554 dehydrovitamin B12, 215 5'-deoxy-8,5'-cycloadenosine, 297 diacetylmonoximeimino diacetyl-

monoximaloiminopropane- 1,3-cobalt, 503

dicyanocobyric acid, 206 4 ',5 -didehy dro-5 '-deoxyaristeromy cin,

297 dimethylated isobacteriochlorins,

123-126 8-epicobalamin, 225 13-epicobalamin, 224 3-episirohydrochlorin, 129 Factor I, 130, 131 heptamethylcobyrinate, iodide

complex, 72 heptamethyl cobyrinic acid, 114 5,7,7,12,14,14-hexamethyl-1,4,8,11 -

tetraazacyclotetradeca-4,11- dienecobalt, 574 iodocobalt(II) cobyrinic acid heptamethyl ester, X-ray crystal-

lographic data, 69 2',3',0-isopropy lidenecyclodihydro-

uridine, 298 Me[14]-diene N4, 574 methyl(aquo)cobyrinic hepta

ferf-alcohol, 278 mono-C-methylated chlorin, 131 neovitamin B12, 34, 224 2,2,7,7,12,13,17,18-octamethyl-

isobacteriochlorin, 136 olefin p-complexes, 534 pentacyanocobaltate, 503 pentadecaalkylcorrin, 237 protoporphyrin IX, 110 rhodium corrin, 34 7,7'(CH3)2 SALEN, 503 secocorrindione, 219 secocorrins, 78, 116

isobacteriochlorins, 135 2,2,7,7,12,13,17,18-octamethyliso-

bacteriochlorin, 136 organocobalt complexes, 245-294

work up of reaction mixtures, cobalt- carbon bond formation, 248 Synthetic analogs, vitamin B12 coenzyme, 332 Synthetic utility, vitamin B12r alkylation,

277

Temperature dependence, cobalamin nmr spectroscopy, 490

Temperature variation, corrin electronic spectra, 348, 407

Template reactions, vitamin B12 total synthesis, 188 Tertiary alkyl, cobaloximes, 254 1,4,8,11-Tetraazacyclotetradecane- cobalt(III): alkyl complexes, photolysis, 271, 524 cobalt-carbon bond, energy, 554 cobalt(II) reaction with alkyl halides, 274

model, vitamin B12 coenzyme, 551 structure, 503, 552 vitamin B12 coenzyme model systems,

551 Tetracarboxylic acid:

circular dichroism, 421 electronic spectrum, 415

Tetracyanoethylene: alkylcobalt complexes, reaction with,

285 cinnamyl(imidazole)cobaloxime, re-

action with, 286 Tetracyclic lactam, vitamin B12 total

synthesis, 174 Tetradehydrocorrin, nomenclature, 19 Tetrahydrochlorins, see Dihydroiso-

bacteriochlorins, Factor I Tetrahydrofolic acid, 528 Tetrakis-(didehydro)corrin, nomenclature,

19 Thallium(III):

alkylation, alkylcobalt complexes, 526 cobalt-carbon bond cleavage, 526

Theoretical considerations, electronic spectrum, 396

Theoretical studies: bridged cation, 557 vitamin B12 coenzyme, enzymic reaction,

557

Structure (Cont'd) sirohydrochlorin, 122-124 sirolactone, 124 spirocyclic intermediate, 119 1,4,8,11-tetraazacyclotetradecane, 503,552 trimethylated isobacteriochlorins, 132,134 uroporphyrin I, 118 uroporphyrin III, 110 uroporphyrinogen III, 110 vitamin B12:

hexacarboxylic acid, 28, 204 c-lactone, 227 monocarboxylic acid, 34

5-phosphate, 24, 34, 170 vitamin B12 coenzyme, 19, 25 vitamin B12r, oxygen complex, 459 yellow corrinoids, gCoPSE, 37-40, 42, 228-230 zinc 15-cyano-2,2,7,7,12,12-hexa-

methylcorrin, 424 see also X-ray structure a-Styrylcobaloxime, thermolysis, 304 b-Substituted alkylcobalamins and alkali, vitamin B12s, 310 meso-Substitution, vitamin B12, 212 Substrate radicals: vitamin B12 coenzyme-mediated re action, 382 vitamin B12r-, intermediate, interaction with, 382 Succinimides: corrin, oxidative cleavage, 217 oxidative cleavage, vitamin B12, 217 Succinyl-CoA, 328 Sulfite and nitrite reductases, isobacterio-

chlorins, 122 Sulfite reductase, siroheme prosthetic

group, 128 Sulfitocobalamin, electronic spectrum, 347,

411 Sulfomethylcyanocobalamin, electronic

spectrum, 413 Sulfonatocobalamin: halogenation, 216 lactam formation, 226 Sulfur extrusion reactions, vitamin B12

total synthesis, 185, 190 Synthesis: alkynylcobalt complexes, 279 1-amino-2-propanol, 13 analysis of reaction mixtures, cobalt- carbon bond,247

Theory: epr spectroscopy, 435 vitamin B12 coenzyme, mechanism of action, 543-582 Thermal cleavage, cobalt-carbon bond, 362 Thermal decomposition, alkylcorrins and

radical scavenging, 512 Thermal dissociation, 1-pheny lethyl-

(pyridine)cobaloxime, cobalt- carbon bond,509

Thermal stability, benzylcobalt complexes, 513

Thermochemical, cobalt-carbon bond dissociation energy determination, 507

Thermodynamics, ligand exchange, table, 5,6-dimethylbenzimidazole, 496

Thermodynamic stability, cobalt-carbon bond,336

Thermolysis: alkylcobalamins, cobalt-carbon bond,

303,525 alkylcobaloximes, 303, 364 alkylcobalt complexes, cobalt-carbon

bond, 525,552 base-on, off, isopropylcobalamin, 552 3-bromopropylcobaloxime, 304 carboxymethylcobaloxime, 304 chloromethylcobaloxime, 304 cobalt-carbon bond, /3-elimination, 304 cyanome hylcobaloxime, 304 cyclohexylcobaloxime, 304 kinetics, isopropylcobalamin, 552 methylcobalamin, 303, 363 neopentylcobalamin, homolytic cleavage,

364,552 1-phenylethylcobaloximes, 304 a-styrylcobaloxime, 304 Thioamide alkylation, vitamin B12 total synthesis, 195 Thiocyanatocobalamin, electronic spectrum, 411 Thiolactam, vitamin B12 total synthesis,

185 Thiolactone, desulfurization, decarbonyla-

tion, vitamin B12 total synthesis, 193

Thiols: alkylcobalamins, 527 alkylcobaloximes, dealkylation, 527 cobalt-carbon bond reductive cleavage, 515

cobalt complexes, reduction, 254 methylcobalamin methyl transfer, 312 photolysis, 5-deoxyadenosine, vitamin B12 coenzyme, 299 Thioredoxin, 545 Thiyl radical, vitamin B12 coenzyme ribo-

nucleotide reductase, 577 L-Threonine, conversion to D-l-amino-2-

propanol, 199 Threonine decarboxylation, [R]-l-amino-

2-propanol, 150 Timing, cobalt-carbon bond biosynthesis,

155-163 Tin(IV), alkylcobalt complexes, alkylation,

527 Torsion around A-D junction, corrin

derivatives, 57 Torsion angles, C(l)-C(19) bond, 56 N-Tosylcytidylcobalamin, reaction wi h cyanide, 306 Total synthesis of vitamin B12: acetoin, 172 amide activation, 192 amide deamination, 191 amide hydrolysis, dinitrogen tetroxide, 192

m-anisidine, 172 Arndt-Eistert, 194 Beckmann rearrangement, 180 (+)camphor, ring C, 174, 184, 193 camphorquinone, 183 Claisen rearrangement, amidoacetal, 184 cobyric acid, 187, 196 coupling, east and west halves, 187 cyanobromide, 1, 172 cyclic 2',3', a-ribazole phosphate, 194 cyclohexyl nitrone, 192 diazomethane esterification, basic

conditions, 193 Diels-Alder, Lewis-acid catalyzed, 183 the eastern half, 183 episulfides, 185 ester ammonolysis, 192 Hagemann's ester, 184 high pressure liquid chromatography,

190 isoxazoles, 175 methylmercury isopropoxide, 185 neocobyric acid, 187, 196 nitrile, hydrolysis, 191 orbital symmetry, 176 orthoamide, 178 oxime hydrolysis, nitrous acid, 170

Trifluoromethylcobalamin, reaction with cyanide, 307

Trifluoromethylcobaloxime, reaction with hydroxide, cob(I)aloxime, 309

1-(2-Trifluoromethylphenyl)imidazole, heptamethylcobyrinate coordination, 495

p-Trifluoromethylphenyl(pyridine)cobaloxime, preparation, 271

3,3,3-Trifluoropropyne, addition to cobalt (I) complexes, 257

Trimethylaminoethylcobalamin, reaction with alkali, 310

Trimethylated isobacteriochlorins: biosynthesis, 132 electronic spectrum, octamethyl ester, 132 incorporation into, cobyric acid, 132 isolation, 132 nmr spectrum, 132 from P. shermanii, 132 structure, 132, 134 Triphenylphosphine cob(II)aloximes, alkyl halides, reactivity towards, 521

Unique biologically, redox chemistry of cobalt, 340

Unsaturated electrophiles, cobalt(I) complexes, addition to, 256

Uro'gen III, see Uroporphyrinogen III Uroporphyrin I, structure, 118 Uroporphyrin III, structure, 110 Uroporphyrinogen I, interaction with

cosynthetase, 118 Uroporphyrinogen III:

biosynthetic precursor, cobyrinic acid, 116 corrin biosynthesis, 139 intact incorporation into corrin, 117 loss of C-20 in corrin biosynthesis, 137 structure, 110

Uroporphyrinogen III cosynthetase, 117 uroporphyrinogen I in teraction with, 118

Uv spectrum, see Electronic spectrum

Vibrational components, electronic spectrum, 403 Vinylcobalamin: electronic spectrum, 346, 415 nmr spectrum (59Co), 490 eaction with acid, 314 Vinylcobaloxime preparation, 261 Vinylcobalt porphyrins, diazoalkanes, preparation, 280

Total synthesis of vitamin B12 (Cont'd) ozonolysis, 174 a-phenylethylamine, resolving agent,

183 (-)-a-phenylethyl isocyanate, 173 photochemical path, 192 regiospecific aldol, 179 retro-Claisen, 174 b-ribazole, 198 D-ribose, 198 ring closure, 190, 196, 197 rings A-D, 172 rings B-C, 183 secocorrins, 196 stereospecific thermal cyclization, 176 sulfur extrusion reactions, 185, 190 template reactions, 188 tetracyclic lactam, 174 thioamide alkylation, 195 thiolactam, 185 thiolactone, desulfurization, decarbonyla tion , 193tricyclic ketone, 173 Transalkylation, cobalt(I) complexes by alkylcobalt(III) complexes, 527 Transcobalamin-II, 156 rrafts-dimethylcobalt(III) complexes,

heavy metal alkylation, 527 trans-effect: cobaloximes, 82 corrin, 80, 330 ligand ordering, 346 nephelauxe ic series, 336 nmr spectroscopy: cobalt complexes, 488 corrin, 487 5,6-dimethylbenzimidazole, 488 methylcorrinoids, 489 spectrochemical series, 336 Transmission, corrin steric effects, 355 Trichloromethylcobalamin photolysis, 303 Tricyclic ketone, vitamin B12 total synthesis, 173 Tricyclohexylphosphincobal(II)Oxime

alkyla ion, alkyl halides, 519 Trie hylaminoethylcobalamin, reaction with c yanide, 307 Trifluoroacetic acid: corrin epimerization, 222 epimerization, neocorrinoids, 222 vitamin B12 , reaction with, 223 Trifluoroethylcyanocobalamin, electronic spectrum, 413

cobalt: incorporation into, 211 reduction by alkali, 226

role in, 333, 335 cobyric acid, conversion to, 197 cobyrinic acid, acid hydrolysis, 230 color and clinical activity, 8 comparison (crystallographic) with vitamin B12 coenzyme (table), 53 comparison to model systems, 504 conjugated system, 238 conversion to:

15-carboxy-15-norcobinamide, 239 cobinamides, 234 cobyric acid, 235 dicyanocobalamin, standard electronic

spectrum, 395 heptamethyl dicyano-5,15-bisnorco-

byrinate, 239 heptamethyl dicyanocobyrinate, 236 pentadecaalkylcorrin, 236

coordination chemistry, 325-392 copper, incorporation into, 211 copper analog, 211 corrin, pentadecaalkyl from, 236 crystal morphology:

pleochroism, 26 refractive index, 26

cyanation, 213 cyanocobalamin, 17 dehalogenation, 217 demetallation, 210 dependent, table:

isomerase reactions, 328 mutase reac ions, 328

deuteration, 212 5,6-dichlorobenzimidazole, X-ray

diffrac ion data, 27 dimethylaminomethylation, 213 electronic spectrum, 207, 393-430,

408,413,415,417 film, 343

electrophilic attack, MO-calculations, 212 epimers, C-3, C-8, C-13, 210 from fermentation, 9 ferredoxin, decyanation, 163 first crystallization, 3 fluorescence, 426 halogenation, c/s-effect, 216, 226 helicity, 209 hexacarboxylic acid: bond angles (tables), 45-53

Vinylcobinamide electronic spectrum, 408 Vinylcyanocobalamin, electronic spectrum, 413 Vinyl ethers: cob(III)aloxime alkylation, 281 cobalt(III) complexes, reaction with, 281 hydroxocobalamin alkyla ion, 281 Vinyl halides, alkylation cobalt(I) complexes, stereochemistry, 260 Vinyl(pyridine)cobaloxime cobalt-carbon bond, bond lengths, 505 Vinyl(pyridine)Z>w(salicylaldehyde)ethylenediiminecobalt cobalt-carbon bond, bond lengths, 505 Visible spectrum, see Electronic spectrum Vitamin B12: absolute configuration, 28 acetamide side chain, 30 acid hydrolysis, 230, 232, 234 addition of chlorine, 216 air dried crystals, 25 amide side chain, nomenclature, 19, 30 animal protein factor, 14 antipernicious anemia factor, 11 aromaticity, 204 biosynthesis:

[5-13C]-aminolevulinic acid, 479 [13 CH3 ] -L-methionine, 480 nmr spectroscopy, 28, 107, 479 [8-13C] porphobilinogen, 480 bond angles (tables), 45-53 bond distances (tables), 45-53 bound to intrinsic factor, electronic

spectrum, 414 bromination, 215 buckling, 208 canonical resonance structures, 205 carboxylic acids, preparation, 231 cell dimensions, 93 cerium(III) hydroxide, cobinamide

from, 236 chemical degradation, 111 chemical formula, 28, 93 chirality, 170 chloramine T, reactions, 215 chlorination, electronic spectrum, 215 chromatography, acid hydrolysis

products, 230 chromic acid oxidation, 218 circular dichroism, 223, 420 cobaloximes, X-ray crystallography,

23-106

Vitamin B12 (Cont'd) bond distances (tables), 45-53 cell dimensions, 92 chemical formula, 92 deuteration, 212 electronic spectrum, 417 folding, 60 space group, 92 structure, 28, 204 torsion around A-D junction, 57 X-ray crystallographic data, 92 X-ray diffraction data, 27 history, 1 hydrolysis, side chain, amide, 33 infrared spectrum, 215 7-irradiation, frozen solution, 318 isolation, 3, 24 lactam:

electronic spectrum, 417 formation, 225, 234 X-ray structure (diagram), 42

lactone: electronic spectrum, 417 formation, 226

c-lactone structure, 227 laser Raman spectrum, 343 luminescence, 426 metal-free, 211 metal replacement, 72 methanolysis, 236 raeso-methyl groups:

oxidation, 239 pKa values, 234

microbiological assay, 7 monocarboxylic acid:

bond angles (tables), 45-53 bond distances (tables), 45-53 cell dimensions, 93 chemical formula, 93 nmr spectrum, 486 space group, 93 structure, 34 torsion around A-D junc ion, 57 X-ray crystallographic data, 93

monocarboxylic acid (E2): neutron diffraction, 33 X-ray diffraction data, 33

X-ray structure (diagram), side chain disorder, 33 nitrosation, 217 nmr spectrum:

13C, biosynthetic studies, 112 13C-enriched, 471, 472, 474, 480

chemical shifts, 485 (13C) table, 476 longitudinal relaxation times, 485 praseodymium, 484

Nobel prize, 2 nomenclature, 17-22 numbering (nomenclature), 18 optical rotatory dispersion, 223 orbital energies, 206 organic solvent soluble, 236 organometallic chemistry, 326 ozonolysis, 218 pentacarboxylic acid, electronic spectrum,

417 peripheral amide groups, reactions, 230-

234 permanganate oxidation, 218, 239 pernicious anemia, 1 5'-phosphate:

bond angles (tables), 45-53 bond distances (tables), 45-53 cell dimensions, 94 chemical formula, 94 planarity deviations, 61 space group, 94 structure, 34 torsion around A-D junc ion, 57 X-ray crystallographic data, 94 X-ray structure (diagram), 34

photolysis, 404 planarity deviations, 61 polarization effects, 402 precursor, vitamin B12 coenzyme, 163 preparation, 215 propionamide side chain, 30 pulse radiolysis, 318 pyrolysis, 239 reaction with:

ascorbic acid, 229 iodine, 226 trifluoroacetic acid, 223

redox chemistry, model systems, 513 rhodium, incorporation into, 211 rhodium analog, 211 selenocyanide

selenium location, 27 X-ray diffraction data, 26 side chain conformations, 208 solvent effects, table, electronic spectrum, 410 space group, 93 steric crowding, 506 structure, 24, 170

laser Raman spectrum, 343 low spin Co(II), 432 methylcobalamin photolysis, 300 methyl radicals:

recombination, 553 scavenger, 300

nmr spectrum, 487 nomenclature, 18 organic radical interaction:

epr spectrum enzymic reaction, 450 separation, 452

oxidation, organic radicals, 376 oxygenation, epr spectrum, 458 oxygen complex, structure, 459 paramagnetic shifts, nmr spectrum, 487 preparation, 439 pulse radiolysis, 318 14N quadrupole interaction, 441 radical recombination, 363 rate, organic radical recombina ion, 525 reaction with alkyl halides table , 274 reduction, organic radicals, 376 reduction of vitamin B12 , ribonucleotide reductase, 434 reductive cleavage, alkylcobalamins, 317 spin-Hamiltonian, table, 441 steric interactions, epr spectrum, 442, 448 substrate radical separation, table,

ethanolamine ammonia- lyase, 454


vitamin B128, 514 X-ray crystallographic data, 69 see also Cob(II)inamides; Cobalt(II)complexes Vitamin B12s: acetylcobalamin, alkali, 311 acidity, 253

adenosine triphosphate, vitamin B12

coenzyme biosynthesis, 523 alkylation:

alkyl halides, 523 kinetics, 259

stereochemistry, 260, 523 alkylcobalamins, photolysis, 302 assay, vitamin B12 coenzyme biosynthesis, 156-161 benzyl bromide, reaction with, 513 coenzyme function, 147 cyclodecyl-l-d-iodide, reaction with, 261

Vitamin B12 (Cont'd) meso-substitution, 212 succinimides; oxidative cleavage, 217 torsion around A-D junction, 57 total synthesis, see Total synthesis,

vitamin B12

water of crystallization, 68 wet crystals, X-ray diffraction data, 25 X-crystallographic comparison, wet and

air-dried, 67 X-ray crystallographic data, 93 X-ray diffraction data, 26 X-ray structure (diagram), 31, 32 yellow corrinoids, preparation, 228-230 zinc, incorporation into, 211 zinc analog, 211

see also Corrin; Cyanocobalamin; Neovitamin B12

Vitamin B12s: reduction, zinc/acetic acid, 365 see also Hydroxocobalamin Vitamin B12b, see Hydroxocobalamin Vitamin B12r- alkylation: alkyl halides, 520 radical intermediates, 520 synthetic utility, 277 alkyl halides, reactivity toward, 521 base-on, off, epr spectrum, 299 benzyl bromide, reaction with, 513 binding to, ribonucleotide reductase, 442 p-bonding, 440 complex with iodide, 522 5'-deoxyadenosyl radical, reaction with, 373 disproportionation, vitamin B128, 253,

514 electronic spectrum, 418 ENDOR,441,442 enzymic formation, 157 epr spectroscopy:

monoclinic model, 440 powder samples, 439, 442 principal axes, 440

single crystals, 442 epr spectrum, oxygenated, 434, 439, 458 formation, Lactobacillus leichmanni,

ribonucleotide reductase, 439 intermediate:

enzymic reaction, 381 interaction with substrate radicals, 382

bond angles, tables, 45-53 bond distances, tables, 45-53 capped cobaloximes, model systems,

533,565 cell dimensions, 93 chemical formula, 93 circular dichroism, 421 cleavage, cobalt-carbon bond, 547-554 cobalamins, conversion to, 156 cobalt-carbon bond: bond lengths, 505 bond strength, 513 cleavage, induc ion, 550

model systems, 551 factors affecting bond dissociation

energy, 531 models for cleavage, 551 protection by side chains, 30, 41 comparison to model systems, 504 conformation, 551 conformational changes, 374 constraint of axial ligands, 41 conversion to methylcobalamin, 163 5- and 6-coordinate, 346 cyanide, D-eo>f/zro-2,3-dihydroxy-4-

pentenal, 305 5'-deadenosyl carbanion and elimination,

cobalt-carbon bond, 549 5'-deadenosyl carbocation, cobalt-carbon

bond,548 5'-deadenosyl radical, cobalt-carbon bond, 548 5'-deoxyadenosine, intermediate, 332, 545 5-deoxyadenosyl ligand, 13C-5'-

deriva ive, 268 5'-2H-deoxyadenosyl ligand, nmr

spectrum,471 m-diaminoplatinum(II), coordination,

497 iol dehydrase:

1,2-dihydroxyalkyl radicals, 571 model systems, 571

dissociation, 472 electrocyclic ring opening, enzymic

reaction, 576 electronic spectrum:

calculations, 398,408 film, 343, 350

enzyme bound, 554 enzymic reaction, table, 546

active site thiol, 555 cobalt-carbon bond cleavage, 507

Vitamin B12s (Cont'd) 5,6-dimethylbenzimidazole, coordina-

tion, 486 dimethyl(bromomethyl)malonate,

reaction with, 564 electronic spectrum, 418 enzymic formation, 158 isopropylcobalamin, ^-elimination,

364 2',3'-isopropylideneadenosy lcobalamin

and r-butoxide, 307 laser Raman spectrum, 343 methylation, N5 -methyltetrahydrofolic

acid, 528 nmr spectrum, 486 nomenclature, 18 nucleophilicity, 251, 523 photolysis, cobalt-carbon bond, 297 pK values, 364 protonation, 364 reaction with aryl halides, 271 b-substituted alkylcobalamins and

alkali, 310 vitamin B12 coenzyme, 549 vitamin B12r, disproportionation, 514 vitamin B12s, 514

see also Cob(I)inamide; Cobalt(I)complexes; Hydridocobalamin Vitamin B12 coenzyme: acid, cobalt-carbon bond cleavage, 312 acid decomposition: cobalt-carbon bond, 366 2,3, dihydroxy-4-pentenal, 312 adenosyl carbene, 549 alkaline decomposition, cobalt-carbon

bond,366 alkylcobalt complexes, model systems,

551,564 aminomutases: model systems, 571 reaction pathways, 573 analogs, 5'-deoxy-5'-halonucleosides,

preparation, 267, 551 base-on, off, electronic spectrum, 350, 357 biosynthesis: eukaryotes, 156 prokaryotes, 156 vitamin B128: adenosine triphosphate, 523 assay, 145-167 bis(salicylaldehyde)ethylenediimineco balt(III), - model systems, 551

VitaminB12 coenzyme (Cont'd) cobalt role, 555 cobalt(II) substrate radical separation,

452 5'-deoxyadenosyl radical, 554 diol dehydrase, 529 dissociation-recombination pathway, 555 epr spectroscopy, 449-458, 558 ethanolamine ammonia-lyase, 529 glutamate mutase, 529 hydrogen abstraction, 554 hydrogen exchange, 449 13C intermediates, epr spectrum, 450 2H intermediates, epr spectrum, 450 kinetic isotope effect, 554 methyImalonyl-CoA mutase, 529 MO-calculations, 557 model systems, 501-541, 528-535,

564-577 oxidative addition, 576 protein role, 555 radical doublet intermediates, 450 rapid reaction intermediate, 455 reaction pathways, 555 reversibility, 545 ribonucleotide reductase, 529 theoretical studies, 557 vitamin B12r as intermediate, 530

enzymic reactions: a-bonded organocorrinoids, 547 cobalt-carbon bond cleavage, 547 electron transfer, 547 hypothetical pathways, 547 organic radicals, 547

enzymic role, olefin n-complexes, 534 epr signals during catalysis, 332 ethanolamine ammonia-lyase:

model systems, 571 olefin ^-complexes, 575 radical ca ions, 573 reaction pathways, 573

flash photolysis, electronic spectrum, 299,376

fluorescent analogs: 2-aminomebularine, 267, 285, 300 2,6-diaminobularine, 300 1,N6-ethenadenosine, 300 formycin, 300

glutamate mutase: acrylate radical, 571 glycinyl radical, 571 model systems, 570

olefin p-complexes, 571 reaction pathways, 571 halogenation, 216 heterolytic cleavage, cobalt-carbon bond,548 hexacarboxylic acid, X-ray structure, 31,32 1 H/2 H exchange, nmr spectrum, 468,

469 homolytic cleavage, cobalt-carbon

bond,548 1,2-hydride shift, 549 hydridocobalamin, 549 hydrophobic pocket, 41 Iodine, cleavage, 316 gamma-irradiation, frozen solution, 318 kinetic isotope effect, [ I-2 H2 ] propane-

1,2-diol, 554 labelled 2H, 3H, 545 lactam formation, 226 laser Raman spectrum, 343 mechanism, role of model systems, 528 mechanism of action:

model systems, 543-582 theory, 543-582

methylcobalamin, conversion to, 163 a-methyleneglutarate mutase:

model systems, 567 reaction pathways, 570

methylmalonyl-CoA mutase: mechanism, 565 model systems, 564

reaction pathways, 565, 566 migration of group X, electron transfer, 555 model systems:

5,7,7,12,14,14-hexamethyl-l,4,8,ll- tetraazacyclotetradeca-4,11- dienecobalt, 377, 501-541, 574

ligand binding, 504 pKa values, 504 redox chemistry, 504 redox potential, 504 bis(salicylaldehyde)ethylenediimine-

cobalt, 551 1,4,8,11-tetraazacyclotetradecane, 551 molecular rearrangements, 545 neutron diffraction, 91 nitrosodurene, reaction with, 298 nmr spectroscopy, 465 nmr spectrum:

chemical shifts, 465 corrin ring, 469

steric crowding, 506 steric effects, ligand equilibria, 341 strain orbital, 560 structural comparison to vitamin B12, 41 structure, 19, 25 substrate radicals, 382 synthe ic analogs, 332 1,4,8,11-tetraazacyclo tetradecane-

cobalt(III), model, 551 thiols, photolysis, 5'-deoxyadenosine,

299 torsion around A-D junction, 57 vitamin B12:

comparison (crystallographic) with, 53 precursor, 163

vitamin B12s, 549 X-ray crystal structure, 550 X-ray diffraction data, 30, 93 X-ray structure, 31, 32, 43, 44 see also Alkylcobalamins

Wagner-Meerwein rearrangement, organic radicals, 556 Water of crystallization, vitamin B12, 68 Work up of reaction mixtures, cobalt- carbon bond synthesis, 248

Xan hocorrinoids: corrin cyclization (peripheral), 225- 230 see also Yellow corrinoids

X-ray crystallographic comparison, wet and air-dried vitamin B12, 25, 67

X-ray crystallographic data, corrin derivative derivatives, 23-106

X-ray crystallography: R-a-cyanoethyl(S-a-methylbenzylamine)-

cobaloxime, racemization, 88 glossary, 97

vitamin B12, cobaloximes 23-106 see also X-ray structure X-ray structure: alkylcobaloximes, 359 anomalous dispersion, 99 cylindrical projection, 55, 100 difference electron density map, 99 direct methods, 99 electron density map, 100 methylcobalamin, complex with bis-

acetylacetone-ethylenediamine, 349 neovitamin B12 , 34, 36 nmr spectroscopy, molecular structure

in solution, comparison to, 482

VitaminB12 coenzyme (Cont'd) 5'-deoxyadenosyl ligand, 468 5,6-dimethylbenzimidazole, 468, 474 praseodymium, 483 propanolamine, 467 protonated, 468 ribose ring, 467

nomenclature, 18 nucleoside analogs, 160 olefin 7r-complexes, 549, 575 organic radicals, 545 oxygen sensitivity, 551 peripheral amide groups, 41 photolysis:

acetaldehyde: ethanolamine, 298 2-ethoxyethylamine, 298 ethylene glycol, 298

electronic spectrum, 296 frozen solution, epr, 299 model for e hanolamine ammonia-

lyase, 298 in presence of nitrosodurene, 298 in presence of thiols, 298 quantum yield, 296, 303, 363

pK values, benzimidazole, 351 planarity deviations, 61 protein role, distortion, 373 protonated, nmr spectrum, 468 protonation, 351 pulse radiolysis, 318 purine nucleosides, 300 ratio, methylcobalamin, 161 reaction with:

alkali, 307 cyanide, 305 a,|3-dibromoethyl acetate, 285 hydrogen cyanide, 306

redox chemistry, model systems, 513 ribonucleotide reductase:

5'-deoxyadenosine, 577 5'-deoxyadenosyl radical, 577 thiyl radical, 577

ribose ring conformation, 550, 554 ring puckering, 41 role of protein, 329 solvent effects, table, electronic spectrum,

410 space group, 93 spin-labelled analogs, 267 spin-lattice relaxation times, 492 stability cobalt-carbon bond, 366 steric compression, X-ray structure, 359

X-ray structure (Cont'd) Patterson map, 98, 101 R factor, 99 rhodium coby rinic acid- tf ,c-diamide, 34side chain disorder, vitamin B12 mono-

carboxylic acid (E2), 33 vitamin B12: lactam, 40 5'-phosphate, 31, 32, 34 vitamin B12 coenzyme: hexacarboxylic acid, 31, 32 steric compression, 31, 32, 43, 44, 359 yellow corrinoids, 38

Yellow corrinoids: ascorbic acid, role in formation, 39, 229 bond angles, distances, tables, 45-53 cell dimensions, 94, 95 chemical formula, 94, 95 dehydration, 229 folding, 60 gCoPSE:

preparation, 40 structure, 42 X-ray diffrac ion data, 40

mechanism of formation, 229 microbiological formation, 228

nmr spectrum, 229, 485 13C nmr spectrum, 229 planarity, deviations, 61 preparation, vitamin B12 , 228-230 radical reactions, vitamin B12, 229 ring structure, 37 space group, 94, 95 structure, 37-40, 228-230 torsion around A-D junction, 57 X-ray diffraction data, 37, 94, 95 X-ray structure, diagram, 38

Zinc: alkylation, trans-dimethylcobalt(III)

complexes, 527 cobalamin reduction, 253 incorporation into: 15 -cy ano-1,2,2,7,7,12,12-hep ta-

methylcorrin, 211 vitamin B12, 211 Zinc/acetic acid, vitamin B123 reduction, 365 Zinc analog, vitamin B12, 211 Zinc 15 -cyano-2,2,7,7,12,12-hexamethy 1- corrin:

electronic spectrum, 424 structure, 423

Zwitterionic: cobalt(III) complexes, 286

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VOLUME 1 Chemistry - daviddolphin.comchemistry, biochemistry, and medicine relating to B J2. Volum e 1 emphasizes chem-istry, biosynthesis, history, and nomenclature; Volume 2 covers