ABSTRACT

An earlier extensive study by Edmund Bowden had demonstrated the importance of using electrodes with hydrophilic surfaces in electrochemical studies of cytochrome c [46]. At that time the cyclic voltammetry of cytochrome c at gold was found to decay with time, but the response could be restored on cleaning the electrode in a soft hydrogen flame that rendered the surface hydrophilic. It is now clear that the lack of stability was due to these samples being chromatographically purified, lyophilized, and then stored at −4°C for later use. This produced oligomeric forms of cytochrome c that fouled metal electrode surfaces. Metal surfaces are more active to adsorption of protein impurities than tin oxide and indium oxide and more easily fouled by protein adsorption.