Gated electron transfer of cytochrome c6 at biomimetic interfaces: a time-resolved SERR study.
The electron shuttle heme protein Cyt-c(6) from the photosynthetic cyanobacterium Nostoc sp. PCC 7119 was immobilized on nanostructured Ag electrodes coated with SAMs that mimic different possible interactions with its natural reaction partner PSI. The structure, redox potential, and electron-transfer dynamics of the SAM-Cyt-c(6) complexes were investigated by TR-SERR spectroelectrochemistry. It is shown that the heterogeneous electron-transfer process is gated both in electrostatic and hydrophobic-hydrophilic complexes. At long tunneling distances, the reaction rate is controlled by the tunneling probability, while at shorter distances or higher driving forces, protein dynamics becomes the rate-limiting event.
Kranich
Anja
A
Institut für Chemie, Technische Universität Berlin. Str. des 17. Juni 135, Sekr. PC, 14, D10623-Berlin, Germany.
Naumann
Hendrik
H
Molina-Heredia
Fernando P
FP
Moore
H Justin
HJ
Lee
T Randall
TR
Lecomte
Sophie
S
de la Rosa
Miguel A
MA
Hildebrandt
Peter
P
Murgida
Daniel H
DH
D001665:Binding Sites; D032701:Biomimetics; D045365:Cytochromes c6 / Q000737:chemistry* / Q000235:genetics; D004583:Electrons; D007700:Kinetics; D008954:Models, Biological; D009154:Mutation; D046937:Nostoc / Q000201:enzymology*; D013059:Spectrum Analysis, Raman; D013499:Surface Properties
D045365:Cytochromes c6