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Protein Dynamics and Cytochrome c:  Correlations between Ligand Vibrations and Redox Activity

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journal contribution
posted on 08.02.2002, 00:00 by Jodie K. Chin, Ralph Jimenez, Floyd E. Romesberg
A recently developed method to directly observe specific protein vibrations, based on deuteration, has been employed to examine the redox-dependent structural and fluctional properties of cytochrome c. The dynamics of the protein-based methionine heme ligand were examined by selectively deuterating the ligand's methyl group. The frequency and line width of the C−D bonds were easily observable and shown to be sensitive to mutation-induced changes in the protein redox potential. However, of seven mutants examined, the C−D line widths were independent of the redox-state of the protein. Therefore, although the ligand dynamics depend on the protein's redox state, there are no detected differences in protein dynamics of the oxidized and reduced proteins.

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