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Towards Protein-based Bio-Electronics
Electron Transfer &
Solid-State Electronic Transport
Fundamental differences and similaritieswith
Mordechai Sheves , Israel PechtNadav Amdursky, Lior Sepunaru
Debora Marchak, Noga Friedman +++++
T U Berlin Nov. 14, 2014
Support
Minerva Foundation, MunichIsrael Min. of Science
Some proteins “survive”partial dehydration
“SOLID-STATE” ELECTRON TRANSPORT (ETP)
substrate / contactlinker layer
Ametal
Idealized cartoon
pad
Lift-off float-on (LOFO) e.g., Au, PEDOT-PSS
Macro-electrode options for soft matter: Hg, “ready-made” metallic pad, evaporated Pb
Hg drop
HgSubstrate
Backcontact
Si
Pb
~1nm
0.2 mm2 106 - 1010 proteins/contact
-1.0 -0.5 0.0 0.5 1.0-3.5
-3.0
-2.5
-2.0
-1.5
-1.0
-0.5
0.0
0.5
1.0
Cur
rent
(A
)
Bias Voltage (on metal) [V]
Az
-1.0 -0.5 0.0 0.5 1.0
1E-12
1E-11
1E-10
1E-9
1E-8
1E-7
1E-6
1E-5
Cur
rent
(A
)
Bias Voltage (on metal) [V]
Az
-1.0 -0.5 0.0 0.5 1.0-3.5
-3.0
-2.5
-2.0
-1.5
-1.0
-0.5
0.0
0.5
1.0
Cur
rent
(A
)
Bias Voltage (on metal) [V]
Apo-Az
-1.0 -0.5 0.0 0.5 1.0
1E-12
1E-11
1E-10
1E-9
1E-8
1E-7
1E-6
1E-5
Cur
rent
(A
)
Bias Voltage (on metal) [V]
Apo-Az
-1.0 -0.5 0.0 0.5 1.0-3.5
-3.0
-2.5
-2.0
-1.5
-1.0
-0.5
0.0
0.5
1.0
Cur
rent
(A
)
Bias Voltage (on metal) [V]
Zn-Az
-1.0 -0.5 0.0 0.5 1.0
1E-12
1E-11
1E-10
1E-9
1E-8
1E-7
1E-6
1E-5
Cur
rent
(A
)
Bias Voltage (on metal) [V]
Zn-Az
Ron et al, JACS 2010
Replacing or removing the Cu ion Zn-azurin or apo-Azurin
Example of ETp measurement: Azurin
Current vs. voltageI-V [ln (I)-V]
@ RT
substrate / contactlinker layer
Ametal
Idealized cartoon
Temperature dependent conduction of “any (> ~2 nm) peptide skeleton”
2 4 6 8 10 12-18
-17
-16
-15
-14
-13
-12
BSA apo-Azurin
Cu
rren
t d
ensi
ty [
mA
/cm
2 ]
1000/T [K-1]
400 300 200 100T [K]
5
Some proteins “survive”partial dehydration
“SOLID-STATE” ELECTRON TRANSPORT (ETP)
10 20 30 40 50 60 70 80 90 1001E-26
1E-24
1E-22
1E-20
1E-18
1E-16
1E-14
1E-12
1E-10
1E-8 macroscopic
Saturated Conjugated Proteins
Cur
rent
Den
sity
(A/n
m2 )
Length (Å)
32 33 34 351E-18
1E-17
substrate / contactlinker layer
Ametal
Idealized cartoon
Amdursky et al., Adv. Mater. 2014
IdealizedCartoons!
We (can) also use nanoscale contacts; let’s take a closer look at such experiments:
A
10 nm
Metallic substrate
2 μm
9
Nanoscale contacts – Azurin
Holo-Az Apo-Az
-0.5 0.0 0.51E-5
1E-4
1E-3
0.01
0.1
1 holo-Az 12nN
holo-Az 6nNapo-Az 12nN
Cur
rent
(nA
)
Bias (V)
apo-Az 6nN
WIS group, ACS Nano 2012Davis group, JMC 2005
10
0 5 10 15 20 250
5
10
15
20
25R
esis
tan
ce (
G
)
Applied force (nN)
0 5 10 150
5
10
15
20
25 WT-bR WT-Azurin
Res
ista
nce
(G
)
Applied Force (nN)
Applied force-dependent conductance
Elastic regime
Plastic regime
Li et al. ACS Nano, 2012Mukhopadhyay et al., ACS Nano (2014)
Azurin
bR
@RT
11
e-
e-
hν
In solid state In solution
ETp ET
Spectroscopy Electrochemistry
e-
How does Electron Transport (ETp) differ from Electron Transfer (ET)?
ETp is measured with electronically conducting electrodes that• are ionically blocking • have delocalized electron systems (affects reorganization energy)
ET is measured without electrodes (or with one ionically conducting, electronically blocking contact)
How does Electron Transport (ETp) differ from Electron Transfer (ET)?
ETp is measured with electronically conducting electrodes that• are ionically blocking • have delocalized electron systems (affects reorganization energy)
ET is measured without electrodes (or with one ionically conducting, electronically blocking contact)
-----------------------------------------------------------------------ETp is measured on proteins outside their natural environment
• in partially “dry” state, with only tightly bound water kept(but with natural conformation closely preserved)
ET is measured with protein in, or partially exposed to solution.
How does Electron Transport (ETp) differ from Electron Transfer (ET)?
ETp is measured with electronically conducting electrodes that• are ionically blocking • have delocalized electron systems (affects reorganization energy)
ET is measured without electrodes (or with one ionically conducting, electronically blocking contact)
-----------------------------------------------------------------------ETp is measured on proteins outside their natural environment
• in partially “dry” state, with only tightly bound water kept(but with natural conformation closely preserved)
ET is measured with protein in, or partially exposed to solution. -----------------------------------------------------------------------ETp: no redox reaction required can study ETp close to equilibrium (@0.05 V)ET : redox reaction required (coupled to ion transport for charge balance)
How does Electron Transport (ETp) differ from Electron Transfer (ET)?
ETp is measured with electronically conducting electrodes that• are ionically blocking • have delocalized electron systems (affects reorganization energy)
ET is measured without electrodes (or with one ionically conducting, electronically blocking contact)
-----------------------------------------------------------------------ETp is measured on proteins outside their natural environment
• in partially “dry” state, with only tightly bound water kept(but with natural conformation closely preserved)
ET is measured with protein in, or partially exposed to solution. -----------------------------------------------------------------------ETp: no redox reaction required can study ETp close to equilibrium (@0.05 V)ET : redox reaction required (coupled to ion transport for charge balance) ------------------------------------------------------------------------BUT ETp may be differ from ET if• pressure is applied (e.g., in SPM)• significant (> 1-1.5 V bias voltage) is imposed• electronic current flows• ………………………… ………
How does Electron Transport (ETp) differ from Electron Transfer (ET)?
• Effect of protein redox activity (for CytC)
• Redox site effect on conduction (for Az)
(also can add redox site in bR)
• Effect of protein-electrode coupling
How does Electron Transport (ETp) differ from Electron Transfer (ET)?
280 320 360 400 440
Nor
mal
ized
Flu
ores
cenc
e (a
.u)
Wavelength (nm)
HSA
HSA-hemin
Case Study – I‘Doping’ serum albumin with hemin
& comparison with Cyt C
Some ETp-ET differences :
• Effect of protein redox activity
-1.0 -0.5 0.0 0.5 1.0
1E-8
1E-7
1E-6
1E-5
1E-4
1E-3
-1.0 -0.5 0.0 0.5 1.0
-0.002
0.000
0.002
0.004
Cur
rent
Den
sity
(A
/cm
2 )
Bias (V)
HSA
HSA-hemin
-1.0 -0.5 0.0 0.5 1.0
-0.002
0.000
0.002
0.004
Cur
rent
Den
sity
(A
/cm
2 )
Bias (V)
CytC HSA-hemin
-1.0 -0.5 0.0 0.5 1.01E-8
1E-7
1E-6
1E-5
1E-4
1E-3
‘Doping’ serum albumin with hemin& comparison with Cyt C
Amdursky et al., PCCP 2013
Some ETp-ET differences :
• Effect of protein redox activity
0 5 10 15 20 25 30 35
-17
-16
-15
-14
-13
-12
ln
(J@
-0.0
5V)
1000/T
HSA
HSA-hemin
0 5 10 15 20 25 30 35-16
-15
-14
-13
-12
HSA-hemin CytC electrostatic
ln(J
@-0
.05V
)1000/T
95 meV
220 meV
-0.6 -0.4 -0.2 0.0 0.2 0.4 0.6
-0.0010
-0.0005
0.0000
0.0005
0.0010
Cur
rent
Bias
-0.4 -0.2 0.0 0.2 0.4 0.6-0.0012
-0.0008
-0.0004
0.0000
0.0004
0.0008
Cur
rent
Bias
HSA-heminCytC
kET ≈ 18 s-1
kET ≈ 5 s-1
‘Doping’ serum albumin with hemin& comparison with Cyt C
Amdursky et al., PCCP 2013
0 10 20 30 40
-12
-10
-8
-6
ln
(J@
0.05
V)
1000/T
100 meV
Fe
0 10 20 30 40-16
-14
-12
-10
-8
-6
-4
ln
(J@
0.05
V)
1000/T
Iron-free CytC
Holo-CytC
Apo-CytC
Cyt C electrostatically bound (physisorbed) to surface
Amdursky et al., JACS 2013
‘Doping’ serum albumin with hemin& comparison with Cyt C
Some ETp-ET differences :
• Effect of protein redox activity
-1.0 -0.5 0.0 0.5 1.0
-0.002
0.000
0.002
0.004
CytC Iron free CytC
Bias (V)
Cur
rent
Den
sity
(A
/cm
2 )
-1.0 -0.5 0.0 0.5 1.0-0.004
-0.002
0.000
0.002
0.004
HSA-hemin HSA-PPIX
Cur
rent
Den
sity
(A
/cm
2 )
Bias (V)
-0.2 -0.1 0.0 0.1 0.2 0.3 0.4 0.5
-200
-100
0
100
200 HSA-hemin HSA-PPIX
Cur
rent
(nA
)
Bias vs. SCE (V)
-0.2 -0.1 0.0 0.1 0.2 0.3 0.4 0.5
-300
-200
-100
0
100
200
300 CytC Iron free CytC
Cur
rent
(nA
)
Bias vs. SCE (V)
The conjugated porphyrin ring, not the Fe ion, is the main ETp mediator,
while in ET the Fe2+/3+ redox process controls the electron transfer.
Amdursky et al., PCCP 2013
‘Doping’ serum albumin with hemin& comparison with Cyt C
)(A
TkE
AeI b
2 4 6 8 10 12
-20
-19
-18
-17
-16
-15
-14
-13
-12
Holo-Az
1000/T [K-1]
ln(J
@+
0.05
V)
Cu ion removal
300 meV
Sepunaru et al., JACS 2011
2 4 6 8 10 12
-20
-19
-18
-17
-16
-15
-14
-13
-12
Apo-Az
Holo-Az
1000/T [K-1]
ln(J
@+
0.05
V)
CASE STUDY-IIAZURINSome ETp – ET differences:
• Redox site effect on conduction
2 4 6 8 10 12-20
-18
-16
-14
-12
ln J
[+
50 m
V]
1000/T [K-1]
400 300 200 100T [K]
Cu-Az
Ni-Az
Co-Az
Zn-Az
TBP
Cu ion replacement
Some ETp – ET differences: • Redox site effect on conduction
AZURIN
0 5 10 15 20 25 30 35
-18
-17
-16
-15
-14
-13
-12holo-Az - Protonated
holo-Az - Deuterated
apo-Az - Deuterated
1000/T
ln(J
@0.
05V
)
apo-Az - Protonated
Amdursky et al., PNAS 2013 and TBP
AZURINSome ETp – ET differences: • Redox site effect on conduction
-1.0 -0.5 0.0 0.5 1.0
-6
-5
-4
-3
-2
-1
0
1
2
3
Cur
rent
(A
)
Bias (V)
Cu+2
Cu+1
2 4 6 8 10 12 14 16
-12
-11
-10
-9
-8
-7
+0.5V +0.2V +0.05V -0.05V -0.2V -0.5V
ln(J
)
1000/T
5 10 15 20 25
-13
-12
-11
-10
-9
-8
-7
+0.5V +0.2V +0.05V -0.05V -0.2V -0.5V
ln(J
)
1000/T
Cu(I) vs. Cu(II) Az
Some ETp – ET differences:
• Redox site effect on conduction TBP
@RT
AZURIN
CASE STUDY-IIIETP WITH CYT C MUTANTS
Amdursky et al., PNAS 2014
with Dmitry Dolgikhd & Rita ChertkovadShemyakin-Ovchinnikov Inst. Bioorg. Chem., RASCarlo Bortolotti, U Modena
Some ETp – ET differences:
• Effect of transport distance ?
0 5 10 15 20 25 30 35
-16.0
-15.5
-15.0
-14.5
-14.0
-13.5
-13.0
-12.5
-12.0
-11.5
Covalent binding (A51C)
Azurin (covalent bound)
Covalent binding (E104C)
Covalent binding (A15C)
Electrostatic binding (WT)
ln
(J@
-0.0
5V)
1000/T
cyto
chro
me
C
Amdursky et al., PNAS 2014
ETP WITH CYT C MUTANTS
Some ETp – ET differences:
• Effect of transport distance ?
26 28 30 32 340
1
2
3
41
2
3
4
5
A51C
G23C
G56CA15C
G37CV11C
E104C
A51C
G23C
G56C
A15C
G37C
V11C
E104C
Cu
ren
t de
nsi
ty @
0.0
5V
(A
/cm
2 )
Length (A)
30K
297K
4 5 6 7 8 9 10 11 120.0
0.5
1.0
1.5
2.0
2.5
3.0
3.5
4.0
A51C
G23C
G56CA15C
G37CV11C
E104C
Cur
ent d
ensi
ty @
0.05
V (A
/cm
2 )
Heme edge-electrode closest proximity (A)
electrode
Cys contact
to electrodeAmdursky et al., PNAS 2014
Some ETp – ET differences:
• effect of partial transport distance
ETP WITH CYT C MUTANTS
0 5 10 15 20 25 30 35
-16.0
-15.5
-15.0
-14.5
-14.0
-13.5
-13.0
-12.5
-12.0
-11.5
Covalent binding (A51C)
Azurin (covalent bound)
Covalent binding (E104C)
Covalent binding (A15C)
Electrostatic binding (WT)
ln
(J@
-0.0
5V)
1000/T
cyto
chro
me
C
Amdursky et al., PNAS 2014
Some ETp – ET differences:
• Protein-electrode coupling
ETP WITH CYT C MUTANTS
Amdursky et al., PNAS 2014
Some ETp – ET differences:
• Protein-electrode coupling
ETP WITH CYT C MUTANTS
0 10 20 30 40 50 60 701E-15
1E-14
1E-13
1E-12
1E-11
1E-10
1E-9
1E-8
1E-7
1E-6
1E-5
nm-scale
Saturated CP-AFM Saturated STM Saturated Electromigration Conjugated CP-AFM Conjugated STM Proteins CP-AFM Proteins STM
Cur
rent
Den
sity
(A
/nm
2 )
Length (Å) Amdursky et al., Progress ReportAdv. Mater. 9-2014
Let’s try to put things in perspective: Protein vs. conjugated & saturated molecule conduction
@RT
32
0 5 10 15 20 250
5
10
15
20
25R
esis
tan
ce (
G
)
Applied force (nN)
0 5 10 150
5
10
15
20
25 WT-bR WT-Azurin
Res
ista
nce
(G
)
Applied Force (nN)
but … remember applied force-dependent conductance
Elastic regime
Plastic regime
W. Li et al. ACS Nano, 2012S. Mukhopadhyay et al., ACS Nano (2014)
0 10 20 30 40 50 60 701E-15
1E-14
1E-13
1E-12
1E-11
1E-10
1E-9
1E-8
1E-7
1E-6
1E-5
nm-scale
Saturated CP-AFM Saturated STM Saturated Electromigration Conjugated CP-AFM Conjugated STM Proteins CP-AFM Proteins STM
Cur
rent
Den
sity
(A
/nm
2 )
Length (Å)
Magnitudes of ETp via proteins more like those via conjugated than those via saturated molecules!!
Let’s try to put things in perspective: Protein vs. conjugated & saturated molecule conduction
Amdursky et al., Progress ReportAdv. Mater. 9-2014
10 20 30 40 50 60 70 80 90 1001E-26
1E-24
1E-22
1E-20
1E-18
1E-16
1E-14
1E-12
1E-10
1E-8 macroscopic
Saturated Conjugated Proteins
Cur
rent
Den
sity
(A/n
m2 )
Length (Å)
32 33 34 351E-18
1E-17
@RT
@RT
ETp allows measuring (also) over long distances; ET explores shorter distances
20 40 60 80 1001E-22
1E-20
1E-18
1E-16
1E-14
1E-12
1E-10
Length (Å)
Spectroscopy Electrochemistry CP-AFM STM Macroscopic
Mea
sure
d/eq
uiva
lent
J (
A/n
m2)
Let’s try to put things in perspective: Compare ET to ETp results on proteins
kET = J . constant
Amdursky et al.,Progress Report
Adv. Mater. 9-2014
@RT
20 40 60 80 1000.01
1
100
10000
1000000
1E8
1E10
1E12
Length (Å)
k ET (
s-1)
STM
CP-AFM
Macroscopic
SpectroscopicElectrochem.
Let’s try to put things in perspective: Compare ET to ETp results on proteins
J = kET / constant
Amdursky et al.,Progress Report
Adv. Mater. 9-2014
@RT
• Need for redox-active proteinsETp does not require redox activity; never?
• Redox site effect on ETpCan be minimal (check with ETp-vibrational spectr.)when is cofactor important (e.g., Cu(I) effect)?
So, from where do we start re. ET vs. ETp ?Proteins are good conduction media; WHY / HOW ?
• Need for redox-active proteinsETp does not require redox activity; never?
• Redox site effect on ETpCan be minimal (check with ETp-vibrational spectr.)when is cofactor important (e.g., Cu(I) effect)?
• Importance of transport distance in ETp ??
So, from where do we start re. ET vs. ETp ?Proteins are good conduction media; WHY / HOW ?
• Need for redox-active proteinsETp does not require redox activity; never?
• Redox site effect on ETpCan be minimal (check with ETp-vibrational spectr.)when is cofactor important (e.g., Cu(I) effect)?
• Importance of transport distance in ETp ??
• Importance of contact – cofactor distance & coupling in ETp:~barrier height; “main-lining” temp.-independent
conduction ?
use/ make proteins with cofactor close to likely contact area;
can we identify coupling spectroscopically: IETS, vibr. spectr.-ETp?
So, from where do we start re. ET vs. ETp ?Proteins are good conduction media; WHY / HOW ?
So, what did we learn till now?
Proteins do not behave as electronic insulators; WHY / HOW ?
(Several) proteins can be investigated in the solid state, while
essentially remaining intact.
Both temperature-independent and thermally activated mechanisms
contribute to conduction.
Redox/prosthetic groups are important for conduction, but ….
different from ET, ETp - conduction doesn’t require redox activity (~~large vs. small polaron
hopping)
Re. peptides…., you can ask us
39
Can the proteins “survive” (partial) dehydration ?
bR568
M412
Photochemical
Thermal
bR Photocycle
AzurinBacteriorhodopsin (bR)
UV-V
is. Ab
sorp
tion
Fluore
scen
ce
400 450 500 550 600 650 700 750 800 850
0.0
0.2
0.4
0.6
0.8
1.0n
orm
aliz
ed A
bso
rban
ce (
A.U
.)
Wavelength (nm)
Bacteriorhodopsin (wet) Bacteriorhodospin (dry ML)
300 400 500 600 700 800
0.0
0.2
0.4
0.6
0.8
1.0
nor
mal
ized
Ab
sorb
ance
(A
.U.)
Wavelength (nm)
Az solution
300 400 500 600 700 800
0.0
0.2
0.4
0.6
0.8
1.0
Az solution dry Az film
300 320 340 360 380
0.0
0.2
0.4
0.6
0.8
1.0
norm
aliz
ed e
mis
sion
inte
nsit
y (A
U)
Wavelength (nm)
Az solution
300 320 340 360 380
0.0
0.2
0.4
0.6
0.8
1.0 Az solution Az film
Ron et al, JACS 2010
UV-V
is.
Ab
sorp
tion
bR dry monolayer - light on bR dry monolayer - light off
bR solution - light off
300 400 500 600 700 800-0.6
-0.4
-0.2
0.0
0.2
0.4
nor
mal
ized
A
bso
rban
ce (
A.U
.)
Wavelength (nm)
bR solution - light on
Diff
ere
nce
Sp
ect
rum
Toolbox
Room temperature, ambient conditions
Monolayer characterization
Conductive substrate
Linker layer
- AFM; TEM Cryo-ED; XRR
- Ellipsometry; UV-Visible Abs.; Fluorescence
- FT-IR; Surface Potential
Preparation of “Solid-State” Protein Junctions
Conductive substrate
Linker layer
• Substrate - smooth ! Metal or Semiconductor
• Linker layer - self-assembled short molecule monolayer with functional terminal group
• Protein layer – should be dense; orientation ??
idealizedcartoon
Si
OO
O
X=NH2, Br, SH
Preparation of “Solid-State” Protein Junctions
Conductive substrate
Linker layer
Electrical top contact
• Substrate - smooth ! Metal or Semiconductor
• Linker layer - self-assembled short molecule monolayer with functional terminal group
• Protein layer – should be dense; orientation ??
• Top contact – deposition and composition compatible with ‘soft’ biological material
idealizedcartoon
Electrical Transport Characteristics: I-V(Mean and SD of 30 junctions)
-1.0 -0.5 0.0 0.5 1.0
-140-120-100-80-60-40-20
020406080
100
Mea
n C
urre
nt (
nA)
Voltage [V]
-1.0 -0.5 0.0 0.5 1.0
-2.5-2.0-1.5-1.0-0.50.00.51.01.52.02.53.03.5
Mea
n C
urre
nt (A
)
Voltage [V]
-1.0 -0.5 0.0 0.5 1.0-14
-12
-10
-8
-6
-4
-2
0
2
4
6
8
Mea
n C
urre
nt (A
)
Voltage [V]
bR Az
BSA
Ron et al, JACS 2010
bRProtein height: 5 nm
AFM Height: 5 nm
Ellipsometry: SiOx: 11-12 Å, organo-silane linkers: 6-7 Å
Monolayer characterization
AzProtein height: 3.6 nm
AFM height: ~ 3.5 nm
rms roughness:0.35-0.4 nm
BSAProtein height: 4 nm
AFM height: ~ 4 nm
rms roughness:0.55-0.6 nm
bR Az BSA
bR Az BSA
bR Az BSA
bR Az BSA
500 nm x 500 nm scans, AFM height images (AC mode)
12 nm 5 nm 5 nm
50 nm 50 nm 50 nm
C o v e r a g e > 90 %
Ron et al, JACS 2010
Recap of experimental approach:probe the proteins sandwiched between two conducting electrodes
Metal/Bridge/Metal configuration.
1) MACROSCOPIC CONTACTS Keep reproducibility in mind:
• Highly doped Si slides
• Controllable growth of thin oxide layer
• Linker layer (‘glue”) <100 >p++ (<0.001 Ohm cm)
SiO2 9-10Å
Propyl-silane linker 6-8Å
400 nm
150 nm
…..
…..
….. …..
…..
contact
…..
intimate 5 µm2 contact to a 0.5 nm2 /monolayer of molecules ? Sure, just contact each grass leaf (~3 cm2) on 70×100 m2
soccer field [Akkerman]
but …
Is also a Cartoon!!
still, higher over-all currents large measuring ability gain
What is the ETp mechanism?
• Hopping• Super-exchange• “2-step tunneling”
• Thermally activated• Temperature independent• Low beta values
ConductanceWidth of
molecular energy levels
Franck-Condon density of states and electron transfer
rate
Conductance via off resonance tunneling is temperature independent.
Electron transfer and conduction relationsCase I: off resonance tunneling
Usually broadened due to interactions
with the leads A. Nitzan – J Phys chem A 2001
Charge transfer upon contact between the systems is not taken
into account!
2 4 6 8 10 12
-20
-18
-16
-14
-12
-10
-8
-6
-4ln
J [
+50
mV
Bia
s]
1000/T [K-1]
400 300 200 100T [K]
Linear regime
Conformational change
Pre-melting transition
Temperature independent
Bacteriorhodopsin
Curr
ent d
ensi
ty [m
A/cm
2 ]
60
2 4 6 8 10 12
-20
-18
-16
-14
-12
-10
-8
Cu
rren
t d
ensi
ty [
mA
/cm
2 ]
1000/T [K-1]
400 300 200 100T [K]
EA=160 meV
WT bR
Apo bR
EA=500 m
eV2 4 6 8 10 12
-20
-18
-16
-14
-12
-10
-8
Cu
rren
t d
ensi
ty [
mA
/cm
2 ]
1000/T [K-1]
400 300 200 100T [K]
Tuning electron transport in Bacteriorhodopsin
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