Abstract
The direct electron transfer reaction of Euglena gracilis cytochrome c-552 at edge-oriented pyrolytic graphite electrodes was determined by cyclic voltammetry to be quasi-reversible, stable and reproducible. The presence of a persistent layer of irreversibly adsorbed cytochrome c-552 on the electrode surface was detected in these experiments. Heterogeneous electron transfer rate constants for both the diffusing and adsorbed forms of the protein are reported, and mechanistic aspects are addressed. The applicability of cytochrome c-552 as a complementarily charged analog of eucaryotic cytochrome c in interfacial bioelectrochemical studies is discussed.
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