Interaction of reduced and oxidized cytochrome c with the mitochondrial cytochrome c oxidase and bc1-complex.
Making use of a hetero-bifunctional reagent (succinimidyl 4-(p-male-imidophenyl)butyrate, SMPB), yeast cytochrome c was linked through a thioether bond to the maleimide group whereas the active N-hydroxy-succinimide ester site of the SMPB was used for the reaction with the primary amino groups of Affi-gel 102. The capacity and stability (also to reducing agents) of the column were greatly improved relative to previous systems. This new gel allowed the study of the interactions of cytochrome c oxidase and reductase with reduced and oxidized cytochrome c. For cytochrome c oxidase a significant difference in the interaction with ferri- and ferro-cytochrome c was observed but no such a difference was seen in the case of cytochrome c reductase.
D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D003574:Cytochrome c Group / Q000378:metabolism*; D014450:Electron Transport Complex III; D003576:Electron Transport Complex IV / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D011808:Quinone Reductases / Q000378:metabolism*
D003574:Cytochrome c Group; D009097:Multienzyme Complexes; D009247:NADH, NADPH Oxidoreductases; D011808:Quinone Reductases; D003576:Electron Transport Complex IV; D014450:Electron Transport Complex III