Structural studies of eukaryotic cytochrome c modified at methionine-65.
1H n.m.r. spectra were recorded in both oxidation states for the following species: tuna cytochrome c, tuna [carboxymethylmethionine-65]cytochrome c, horse cytochrome c and horse [homoserine-65]cytochrome c. The experiments give the assignments of the singlet methyl resonances of methionine-65 and the N-terminal acetyl group. The modification at methionine-65 is shown to cause an extremely small structural perturbation to one part of the molecule close to the site of modification.
D000818:Animals; D003574:Cytochrome c Group; D006714:Homoserine; D006736:Horses; D009682:Magnetic Resonance Spectroscopy; D008715:Methionine; D010084:Oxidation-Reduction; D013045:Species Specificity; D014413:Tuna
D003574:Cytochrome c Group; D006714:Homoserine; D008715:Methionine