Electron‐transfer dynamics of cytochrome C: A change in the reaction mechanism with distance
Angewandte Chemie International Edition, 2002•Wiley Online Library
and the coverage of cytochrome corresponds to about 10% of the pyridine sites, which is
less than 1% overall. The nearly ideal quality of the voltammograms stands in strong
contrast to that reported with pure layers of pyridine-terminated alkanes,[3a] for which the
voltammetry studies showed there to be severe asymmetry in the redox rates and significant
inhomogeneity. The homogeneous behavior of the voltammetry that is observed for the
mixed films indicates that the protein does not denature.[4] Spectroscopic studies are …
less than 1% overall. The nearly ideal quality of the voltammograms stands in strong
contrast to that reported with pure layers of pyridine-terminated alkanes,[3a] for which the
voltammetry studies showed there to be severe asymmetry in the redox rates and significant
inhomogeneity. The homogeneous behavior of the voltammetry that is observed for the
mixed films indicates that the protein does not denature.[4] Spectroscopic studies are …
and the coverage of cytochrome corresponds to about 10% of the pyridine sites, which is less than 1% overall. The nearly ideal quality of the voltammograms stands in strong contrast to that reported with pure layers of pyridine-terminated alkanes,[3a] for which the voltammetry studies showed there to be severe asymmetry in the redox rates and significant inhomogeneity. The homogeneous behavior of the voltammetry that is observed for the mixed films indicates that the protein does not denature.[4] Spectroscopic studies are underway to characterize the adsorbed cytochrome and will be reported elsewhere.
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