Protein dynamics and cytochrome c: correlations between ligand vibrations and redox activity.
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.
Chin
Jodie K
JK
Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Jimenez
Ralph
R
Romesberg
Floyd E
FE
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
D003574:Cytochrome c Group; D005296:Ferrous Compounds; D008024:Ligands; D003903:Deuterium