Redox Transformations of Proteins and Enzymes on Electrodes

Thus the conformational behavior of proteins at the electrode-electrolyte interface is presumably determined by the properties of this boundary surface tension, charge, hydrophobicity, and chemidal structure. It is to be remembered, however, that the above picture presents only a qualitative character, because results of direct structural (for instance, spectral) investigations into protein conformation at the interphase boundary are not available. 

Some ecific examples of the study of electrochemical behavior of proteins and enzymes are given below. 

Despite certain differences of opinion regarding the mechanism of the electrode reaction of cytochrome, highly significant is the fact that there is a direct exchange of electrons between the protein molecule s active center and the electrode. 

It has been reported that a reversible one-electron transformation of cytochrome c occurs on an indium oxide electrode. Cytochrome c yields quasi-reversible maxima at EhO 0. 25 V on a gold electrode in the presence of 4,4 -bipyridine. 

The electrode behavior of certain other cytochromes has also been investigated. It has been shown that cytochrome C3 yields a reversible wave on the mercury electrode, the reaction involving four successive transitions of 

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