Abstract
Surface-enhanced resonance Raman (SERR) spectroscopy was employed to study cytochrome c″ (Cyt-c″) adsorbed on a silver electrode. Depending on the electrode potential, the adsorbed Cyt-c″ exists in various conformational states including the native six-coordinated low spin (6cLS) and the five-coordinated high spin (5cHS) configurations of the oxidised and reduced forms, respectively. In contrast to Cyt-c″ in solution, two additional species are found for the adsorbed protein: a 5cHS ferric and a 6cLS ferrous form. The latter species which is only detected at potentials close to the redox potential is ascribed to an intermediate state of the redox process that most likely involves a coupling of electron transfer and ligand (de)protonation.
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