Organic & Biomolecular ChemistryThe epoxide substrates used to model the mechanisms were the racemic styrene oxide (rac-SO) and its racemic para nitro substituted derivative (rac-p-NSO,

Organic&BiomolecularChemistry

SUPPORTINGINFORMATION

ExploringtheoriginsofselectivityinsolubleEpoxideHydrolasefromBacillusmegateriumEilaSerrano-Hervás,aMarcGarcia-Borràs*bandSílviaOsuna*a

SUPPORTINGINFORMATION

Electronic Supplementary Material (ESI) for Organic & Biomolecular Chemistry.This journal is © The Royal Society of Chemistry 2017

SUPPORTINGINFORMATION Organic&BiomolecularChemistry

Computationalmethods

Full geometry optimizationswere performedwith the hybrid DFT B3LYP functional1, 2 and the 6-31G(d)basis set3, 4 basis set using Gaussian 09,5 awidely accepted level of theory for studyingmechanisms oforganicreactions.6,7Theeffectsoftheactivesiteenvironmentoftheproteinwereimplicitlyincludedinallcalculations using the Conductor-like Polarizable ContinuumModel (CPCM)8, 9 with diethyl ether as thesolvent (ε=4). The transition states (TS) were located by using a Bofill update TS search on a reducedpotentialenergysurface.10Analyticalfrequencycalculationswereperformedatthesameleveloftheoryasthegeometryoptimizationstoobtainthezeropointenergies(ZPE).ThenatureofthestationarypointswasdeterminedineachcaseaccordingtotheHessianmatrixeigenvalues.Wehavealsocheckedthatimaginaryfrequencies exhibit the expected motion, while transition states have also been verified by intrinsicreactioncoordinate (IRC)calculations.Moreaccurateenergieswereobtainedbysingle-pointcalculationsincluding the DFT hybrid B3LYP-D3BJ dispersion correctionwith the larger 6-311+G(2d,2p) basis set. AllenergiesareZPE-corrected.Active sitemodel. The quantum chemical model used has been devised based on themost populatedcluster from a 1000-ns MD simulation on the alkyl-enzyme intermediate (Int1, see full details of MDsimulationbelow).ThestartingstructurewasobtainedfromtheX-raycrystalstructureofwild-typeBmEHfromthePDBstructure:4NZZ.Theclustermodelconsistsof:Asp239-His267-Asp97catalytictriad,thetwoactiveTyr144andTyr203,thenucleophilicwatermoleculeandtwohydrogenbondedamidebonds(Gly29-Phe30 and Phe30-Pro31 from the oxyanion motif HGFP). In addition, Trp98, Leu168, Met145, Thr241,Pro240 residues were also included to appropriately describe the shape of the active site cavity ofBmEH4NZZenzyme.Allaminoacidsweretruncatedattheα− orβ−carbon,exceptforthetyrosines,whicharemodelledasphenolsandforthePro240, inwhichonlytheα− anditsside-chaincarbonattachedareincludedtoproperlysimulate theconformational rigidityofproline.Atoms inblack inFigure2are thosemaintained fixed to their initial Cartesian coordinates during the optimizations. Hydrogen atoms wereincludedmanually based either on literature and BmEH4NZZ active site rearrangement, resulting the twoaspartate Asp97 and Asp239 active site residues modelled as in the negatively charged state, whereasHis267wasmodelled in the neutral form, obtaining a quantummodelwith an overall charge of -2 (seeFigure2).

Theepoxidesubstratesusedtomodelthemechanismsweretheracemicstyreneoxide(rac-SO)anditsracemicparanitrosubstitutedderivative(rac-p-NSO,clustermodelsof195and197atoms,respectively).Toexploretheoriginsoftheenantio-andregioselectivityofBmEHandtheeffectofthepresenceoftheNO2group,allplausiblereactionmechanismshouldbeconsidered.Thus,atotalof16reactionpathwaysneedtobecomputedtotakeintoaccountthatEHshydrolysisofrac-epoxidescantakeplaceviaattackoneithercarbonatomofeachenantiomer,butalsotwopossiblebindingorientationsofthesubstrateonthebasisoftheproposedBmEHactivesitetunnel.11Thetwopossiblebindingposesarisefromtheorientationof the phenyl moiety of the substrate towards either region 1 (r1) placing the phenyl moiety close toHis267,orregion3(r3)whenitispointingtowardsTrp98(seeFigure1and2).

MolecularDynamics of the alkyl intermediate.1000nsMD simulation in explicitwaterwas performedusingAMBER16package12inourin-houseGPUclusterGalatea.Parameters for the non-standard alkyl-intermediatewere generatedwithin theantechambermodule ofAMBER16 using the general AMBER force field (GAFF),13with partial charges set to fit the electrostaticpotentialgeneratedattheHF/6-31G(d)levelbytherestrainedelectrostaticpotential(RESP)model.14ThechargeswerecalculatedaccordingtotheMerz-Singh-Kollmanscheme15,16usingGaussian09.5Aminoacidprotonation states were predicted using the H++ server (http://biophysics.cs.vt.edu/H++).17 Then, thecovalentlymodifiedenzyme(PD:4NZZ)wassolvatedinapre-equilibratedtruncatedcuboidboxwitha10-ÅbufferofTIP3P18watermoleculesusingtheAMBER16 leapmodule,resulting intheadditionof∼9,000solventmolecules.Thesystemswereneutralizedbyadditionofexplicitcounterions(Na+).Allsubsequentcalculations were done using the widely tested Stony Brook modification of the Amber 99 force field(ff99SB).19A two-stage geometry optimization approachwas performed. The first stageminimizes the positions ofsolventmoleculesand ions imposingpositional restraintsonsolutebyaharmonicpotentialwitha forceconstantof500kcal·mol−1·Å−2,andthesecondstageisanunrestrainedminimizationofalltheatomsinthesimulationcell. The systemsaregentlyheatedusing six50-ps steps, incrementing the temperature50Keach step (0–300 K) under constant volume and periodic boundary conditions. Water molecules weretreatedwith the SHAKEalgorithm such that the anglebetween thehydrogenatoms is kept fixed. Long-rangeelectrostaticeffectsweremodeledusingtheparticle-mesh-Ewaldmethod.20

Organic&BiomolecularChemistry SUPPORTINGINFORMATION

An 8-Å cutoff was applied to Lennard-Jones and electrostatic interactions. Harmonic restraints of 10kcal·mol-1 were applied to the solute, and the Langevin equilibration scheme was used to control andequalize the temperature. The time stepwas kept at 1 fs during the heating stages, allowing potentialinhomogeneities to self-adjust. Each systemwas thenequilibratedwithout restrains for 2 nswith a 2-fstime-stepataconstantpressureof1atmandtemperatureof300K.AfterthesystemswereequilibratedintheNPTensemble, 1µsMD simulationwasperformedunder theNVTensemble andperiodic-boundaryconditions.

FigureS1.Representationof theoverlayof themostpopulated1µsMDBmEH simulation (in teal), the clustermodel structuresTS1-S-C1-r1 (ingreen)andInt1-S-C1-r1(inpurple).

FigureS2.B3LYP-D3BJ/6-311+g(2d,2p)//6-31g(d)levelcorrespondingtothedifferentstepsoftheBmEHmechanismofactionfor(R)-p-NSOsubstrateorientedtowardsregion3fortheattackatthebenzylicpositon(C1):A)epoxideringopening(TS1-R-C1-r3),B)alkyl-enzymeintermediate(Int1-R-C1-r3),C)hydrolysisofalkyl-enzymeintermediate(TS2-R-C1-r3),D)tetrahedralintermediate(Int2-R-C1-r3),E)dissociationoftetrahedral(TS3-R-C1-r3)andF)productcomplex(Prod-R-C1-r3).AlldistancesareinÅ.Activesitepocketresiduesareshownastransparentsticksandspheresandnon-polarhydrogenatomsareomittedforclarity.Atomsinblackspheresandasterisksarethosemaintainedfixed.

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FigureS3.Non-covalentinteractionsrepresentationoftransitionstatesA)TS2-S-C1-r1andB)TS3-R-C1-r1forthemostfavouredattackof(S)-p-NSOhydrolysisusingtheNCIplotcomputationaltool.21,22NCIsurfaceshowintermolecularinteractionsbetweentheepoxidesubstrateandtheactivesiteresiduesincludedintheCMmodel.Allresiduesarerepresentedasballsandsticksandthetwopossibleorientationsofeachsubstrateisindicatedfor each case (region 1, His267 and region 3, Trp98). Only the most important catalytically residues are labelled regarding BmEH (PDB: 4NZZ)numberingandnon-polarhydrogenarenotshownforclarity.Greyarrowsareusedtohighlightthemostimportantnoncovalentinteractions.Themostimportantresiduesareframed.

FigureS4.EnergyprofilesatB3LYP-D3BJ/6-311+g(2d,2p)//B3LYP/6-31g(d,p)leveloftheoryforallpossibleBmEH-mediatedepoxiderac-SOhydrolysisoutcomes.Allenergiesareinkcal·mol-1andreferencedtothelowestenergyRCforeachenantiomer,RC-S-SO-r1andRC-R-SO-r1,respectively.

TS2-S-C1-r1 TS3-R-C1-r1

A B


FigureS5.B3LYP-D3BJ/6-311+g(2d,2p)//6-31g(d) levelcorrespondingtothedifferentstepsof theBmEHmechanismofactionfor(S)-SOsubstrateorientedtowardsregion1fortheattackatthebenzylicpositon(C1):A)epoxideringopening(TS1-S-SO-C1-r1),B)alkyl-enzymeintermediate(Int1-S-SO-C1-r1),C)hydrolysisofalkyl-enzymeintermediate(TS2-S-SO-C1-r1),D)tetrahedralintermediate(Int2-S-SO-C1-r1),E)dissociationoftetrahedral(TS3-S-SO-C1-r1)andF)productcomplex(Prod-S-SO-C1-r1).AlldistancesareinÅ.Activesitepocketresiduesareshownastransparentsticksandspheresandnon-polarhydrogenatomsareomittedforclarity.Atomsinblackspheresandasterisksarethosemaintainedfixed.

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Cartesiancoordinatesofallanalyzedstructures

RC-S-r1C3.1218250.913373-6.063232C2.372582-0.417722-6.004175O2.344332-1.174090-6.982210N1.735075-0.702694-4.831440C1.026467-1.966736-4.654905C-0.493547-1.735401-4.577687O-0.951315-0.877462-3.799086C1.522852-2.710617-3.384626C1.002523-4.129639-3.291613C1.723567-5.188832-3.863475C-0.224314-4.416303-2.675992C1.232115-6.495198-3.829929C-0.721530-5.720787-2.643276C0.003732-6.764954-3.222321N-1.312504-2.480843-5.349308C-0.958062-3.584905-6.275020C-2.315112-4.227240-6.594022C-3.300728-3.052401-6.497747C-2.768591-2.244730-5.309206C3.4880353.897733-2.592967C4.8351793.163777-2.656219O5.8916973.804622-2.614047C2.2127643.125073-2.956444C1.9404361.998715-1.944473O1.7155282.348685-0.759999O2.0489610.789946-2.349245N4.8113761.805811-2.728593C6.0180180.992573-2.643603C5.752655-0.346018-1.926635C5.414723-0.222072-0.466597C4.1718290.0286100.064797C6.327551-0.2993080.648556C5.562909-0.0889291.833877C7.709452-0.5329530.771738N4.2548680.1007771.443055C6.139374-0.1035823.108898C8.286179-0.5491842.037136C7.509016-0.3348743.194906C-2.491924-4.5770034.960473C-2.048674-4.4937403.640281C-2.407613-3.4539095.788696C-1.526997-3.3011213.140469C-1.889279-2.2550695.303847C-1.449380-2.1784733.976151O-0.949371-0.9838833.544771C1.044858-6.5524236.686135C1.618405-5.2246617.195408C1.728955-4.1777886.083408C-8.378052-2.297238-3.100019C-8.282150-3.822001-2.978299C-6.886956-4.414017-3.259372C3.660950-5.7227432.007463C3.731420-4.3278262.059706C2.557238-6.3234761.393920C2.714857-3.5372781.516453C1.536412-5.5476700.848349C1.608908-4.1485600.911413O0.576322-3.4489180.361111C-4.8631578.0049722.166770C-3.6058158.3229921.353399

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Organic & Biomolecular ChemistryThe epoxide substrates used to model the mechanisms were the racemic styrene oxide (rac-SO) and its racemic para nitro substituted derivative (rac-p-NSO,