Comparative solvent perturbation of horse heart cytochrome c and Rhodospirillum rubrum cytochrome c2.
J Biol Chem, 1979/5/25;254(10):4110-3.
PMID: 220233
Abstract
The extent of exposure of heme to solvent in horse heart cytochrome c and Rhodospirillum rubrum c2 was investigated to determine whether a correlation exists between the properties of these oxidation-reduction proteins and their heme environments. Solvent perturbation absorption difference spectra were measured using ethylene glycol, glycerol, and sucrose at concentrations between 0 and 30%. Cytochrome c appears to exhibit a somewhat greater extent of heme exposure than cytochrome c2 for both the oxidized and reduced states. These results suggest that the lower oxidation-reduction potential of cytochrome c may in part be due to a greater extent of exposure of the heme. The oxidized state of both proteins appears to exhibit a greater exposure than that of the reduced state which is consistent with a more favorable environment for the charge on the ferric heme coordination center.
MeSH terms
Animals; Cytochrome c Group; Ethylene Glycols; Glycerol; Heme; Horses; Myocardium; Oxidation-Reduction; Protein Conformation; Rhodospirillum rubrum; Solvents; Sucrose
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