title: Electron transfer reactions of cytochrome c confined within erythrocyte ghosts.
abstract: We have prepared and characterized resealed erythrocyte ghosts in which the only discernible pigment is cytochrome c. The resealed ghosts have the normal orientation and are free of 'leaky' species; they are stable and can be maintained at 4 degrees C for many days without lysis. The internal cytochrome c participates in redox reactions with both soluble and insolubilized cytochrome c present externally, and with external cytochrome b5. No reaction was observed with plastocyanin, cytochrome c oxidase or NADPH-cytochrome c reductase. A study has been made of the reaction of the internal cytochrome c with the low molecular weight reductants, ascorbate and glutathione. Complex kinetics are observed with both reagents: with ascorbate the results are best explained by assuming the existence, in the membrane, of a redox-active species able to undergo dedimerization. A protein bound disulfide bond would satisfy the requirement.
mesh_terms: D001205:Ascorbic Acid / Q000494:pharmacology; D003574:Cytochrome c Group / Q000378:metabolism*; D003580:Cytochromes / Q000032:analysis; D004579:Electron Transport; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005978:Glutathione / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D010084:Oxidation-Reduction; D013053:Spectrophotometry; D013997:Time Factors
chemical_list: D003574:Cytochrome c Group; D003580:Cytochromes; D005978:Glutathione; D001205:Ascorbic Acid