Cytochromes, their electrochemical behavior

Heme proteins have also been adsorbed to TCO surfaces as modifiers of their electrochemical properties. These adsorption processes are undoubtedly a combination of electrostatic forces, H-bonding, and metal ion coordination in the TCO surface, and produce reasonably robust and active modifying layers. Cytochrome C (cyt C) has been the most extensively studied adsorbed heme protein. Hawkridge and coworkers have examined the electrochemical behavior at gold, platinum, and metal oxide electrodes [81]. Electron transfer rates as high as 10 cm were obtainable at ITO electrodes. Bowden and coworkers have determined that the... 

Bianco and Haladjian recently reported the polarographic behavior of cytochrome Cy, also denoted C55,5- from Desulfuromonas acetoxidans. This molecule contains three hemes, has a molecular weight of ca. 9,800 daltons, and a formal potential of ca. -0.19 V. Their results indicated that the electrochemical responses of cytochrome C3 and cytochrome Cy are very similar. 

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