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Redox Equilibria of Cytochrome C3 Immobilised on Self-Assembled Monolayers Coated Silver Electrodes

Cytochromes c3 are soluble electron transfer proteins in the periplasm of sulphate-reducing bacteria. They act as electron-proton couplers between hydrogenase and the electron transfer chain of sulphate respiration. In this work, cytochrome c3 (Cyt-c3) obtained from both Desulfovibrio vulgaris and Desulfovibrio gigas, is electrostatically adsorbed on Ag electrodes coated with self-assembled monolayers of 11-mercaptoundecanoic acid. The redox equilibria of the adsorbed tetraheme protein are studied by surface enhanced resonance Raman spectroscopy (SERRS). The quantitative analysis of the SERR spectra, which were measured as a function of the electrode potential, allows determining the redox potentials for the individual hemes of Cyt-c3. The values obtained of the redox potentials are compared with the data provided by NMR experiments and by molecular dynamics simulation studies of the electrostatically bound protein on a coated electrode. It is found that immobilisation causes substantial shifts of the redox potential, which would have an impact on the intramolecular electron flow.