Cytochrome c electron transfer reaction

Gray HB, Winkler JR (1996) Electron transfer in proteins. Annu Rev Biochem 65 537 Fedurco M (2000) Redox reactions of heme-containing metalloproteins dynamic effects of self-assembled monolayers on thermodynamics and kinetics of cytochrome c electron-transfer reactions. Coord Chem Rev 209 263... 

Pappa, H. S. Tajbaksh, S. Saunders, A. J. Pielak, G. J. Poulos, T. L., Probing the cytochrome c peroxidase-cytochrome c electron transfer reaction using site specific cross-ttnking. Biochemistry 1996, 35,4837-4845. 

It is apparent that the cytochrome c electron transfer reaction at mercury electrodes is complex and dependent on a number of parameters. The adsorption of cytochrome c at mercury is in and of itself a complicated process. The formation of the first monolayer is rapid and chemically irreversible. 

In a recent report, it was demonstrated that adsorption of 4,4 -bipyridine on platinum led to quasi-reversible rates of electron transfer with cytochrome c as evidenced by cyclic voltammetry. However, the concentration of 4,4 -bipyridine required to produce this electrochemical response was five times that which is required at gold electrodes. This difference was ascribed to the difference in the tendency of 4,4 -bipyridine to adsorb at gold and platinum electrodes. These results indicate that the use of 4,4 -bipyridine may be applicable to other solid electrodes as well for the study of cytochrome c electron transfer reactions. 

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