Protein dynamics and cytochrome c: correlations between ligand vibrations and redox activity

J.K. Chin, R. Jimenez, F.E. Romesberg, J. Am. Chem. Soc. (Comm.) (2002) 124:1846–1847.
pubpic2002chinThe 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.