On the electron transfer mechanism between cytochrome c and metal electrodes. Evidence for dynamic control at short distances

Article Abstract:

The mechanism of heterogeneous electron transfer of the immobilized protein is studied using cyclic voltammetry and time-resolved surface-enhanced resonance Raman spectroelectrochemistry. Measurements of the temperature, distance, and overpotential dependencies of the electron transfer rates indicate a change of mechanism from a tunneling controlled reaction at long distances to a solvent/protein friction controlled reaction at smaller distances.

Analysis, Electric properties, Spectra, Raman spectroscopy, Voltammetry, Structure

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Surface-enhanced resonance Raman Spectroscopic and electrochemical study of cytochroime c Bound on electrodes through coordination with pyridinyl-terminated self-assembled manolayers

Article Abstract:

The cytochrome c (cyt-c) represents a perfect model protein, as its three- dimensional structure is well characterized and a large body of experimental data has been accumulated with heterogeneous and homogenous electron transfer reactions. The surface-enhanced resonance ram (SERR) spectroscopy probes all absorbed cyt-c species CV measurements indicate only the electronically active sub states.

Proteins, Spectrum analysis, Spectroscopy, Electrodes, Raman effect

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