title: Protein dynamics and cytochrome c: correlations between ligand vibrations and redox activity.
abstract: 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.
authors.affiliation: Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
authors.forename: Jodie K
authors.initials: JK
authors.lastname: Chin
authors.forename: Ralph
authors.initials: R
authors.lastname: Jimenez
authors.forename: Floyd E
authors.initials: FE
authors.lastname: Romesberg
mesh_terms: D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism; D003903:Deuterium; D005296:Ferrous Compounds / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D014732:Vibration
chemical_list: D003574:Cytochrome c Group; D005296:Ferrous Compounds; D008024:Ligands; D003903:Deuterium