Direct electrochemistry of protein-protein complexes involving cytochrome c, cytochrome b5, and plastocyanin.
The direct electrochemistry of the cytochrome c/cytochrome b5 and cytochrome c/plastocyanin complexes has been investigated at edge-plane graphite and modified gold electrode surfaces, which are selective for one of the two components of the complex. Electrochemical response of one protein at an otherwise electrostatically unfavorable electrode surface was achieved in the presence of the other protein, and the calculated heterogeneous electron-transfer rate constant and diffusion coefficient were found to be in good agreement with the values determined previously from the electrochemistry of the individual proteins [Armstrong, F. A., Hill, H. A. O., & Walton, N. J. (1988) Acc. Chem. Res. 21, 407 and references therein]. A dynamic model of the protein-protein-electrode ternary complex is proposed to explain the promotion effect, and this model is supported by a study comparing the electrochemical responses of covalent and electrostatic cytochrome c/plastocyanin complexes. It is also suggested that the behavior of protein-protein complexes at electrode surfaces could be related to that of the complexes associated with biological membranes.
Bagby
S
S
Inorganic Chemistry Laboratory, University of Oxford, U.K.
Barker
P D
PD
Guo
L H
LH
Hill
H A
HA
D003574:Cytochrome c Group; D015786:Cytochromes b5; D004563:Electrochemistry; D004566:Electrodes; D008954:Models, Biological; D010940:Plant Proteins; D010970:Plastocyanin; D011487:Protein Conformation
D003574:Cytochrome c Group; D010940:Plant Proteins; D010970:Plastocyanin; D015786:Cytochromes b5