On the electron transfer mechanism between cytochrome C and metal electrodes. Evidence for dynamic control at short distances.
Cytochrome c was coordinatively bound to self-assembled monolayers of pyridine-terminated alkanethiols on Au and Ag electrodes. The mechanism of heterogeneous electron transfer of the immobilized protein was investigated by cyclic voltammetry and time-resolved surface-enhanced resonance Raman spectroelectrochemistry. The temperature, distance, and overpotential dependencies of the electron transfer rates indicate a change of mechanism from a tunneling controlled reaction at long distances (thicker films) to a solvent/protein friction controlled reaction at smaller distances (thinner films).
Yue
Hongjun
H
Chemistry Department, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Khoshtariya
D
D
Waldeck
D H
DH
Grochol
J
J
Hildebrandt
P
P
Murgida
D H
DH
D000465:Algorithms; D000818:Animals; D045304:Cytochromes c / Q000737:chemistry*; D004553:Electric Conductivity; D004563:Electrochemistry; D004566:Electrodes; D004579:Electron Transport; D004583:Electrons; D006736:Horses; D008670:Metals / Q000737:chemistry*; D010084:Oxidation-Reduction; D012997:Solvents / Q000737:chemistry; D013059:Spectrum Analysis, Raman; D013696:Temperature; D013816:Thermodynamics; D014783:Viscosity
D008670:Metals; D012997:Solvents; D045304:Cytochromes c