Electron transfer reactions of metalloproteins at peptide-modified gold electrodes.
The electron transfer reactions of four small redox proteins, cytochrome c. ferredoxin, plastocyanin and azurin, have been investigated at novel peptide-modified gold electrodes. These proved to be effective and selective in facilitating electron transfer. Good, quasi-reversible electron transfer was achieved selectively at different peptide-protein configurations by changing the pH or the ionic strength of the solution. The use of peptides as promoters for protein electrochemistry opens up the possibility of designing very specific electrode surfaces for larger molecules like enzymes.
Barker
P D
PD
Inorganic Chemistry Laboratory, Oxford, England.
Di Gleria
K
K
Hill
H A
HA
Lowe
V J
VJ
D001400:Azurin / Q000032:analysis; D003574:Cytochrome c Group / Q000032:analysis; D004563:Electrochemistry; D004566:Electrodes; D004579:Electron Transport; D005288:Ferredoxins / Q000032:analysis; D006046:Gold; D006863:Hydrogen-Ion Concentration; D008667:Metalloproteins / Q000032:analysis*; D010084:Oxidation-Reduction; D010455:Peptides; D010970:Plastocyanin / Q000032:analysis; D013499:Surface Properties
D003574:Cytochrome c Group; D005288:Ferredoxins; D008667:Metalloproteins; D010455:Peptides; D001400:Azurin; D006046:Gold; D010970:Plastocyanin