Interaction of cytochrome c with reaction centers of Rhodopseudomonas sphaeroides R-26: determination of number of binding sites and dissociation constants by equilibrium dialysis.
The number of binding sites and dissociation constants of cytochrome c (horse heart) and cytochrome c2 (Rhodopseudomonas sphaeroides) to reaction centers of Rhodopseudomonas sphaeroides R-26 was determined by equilibrium dialysis. One binding site was found for both cytochromes. The dissociation constants (10 mM Tris-HCl, pH 8.0) were approximately 0.4 microM and approximately 1.0 microM for cytochrome c and cytochrome C2 respectively. Oxidized and reduced forms of both cytochromes bound to reaction centers with approximately equal affinity.
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D003574:Cytochrome c Group / Q000378:metabolism*; D003956:Dialysis; D007700:Kinetics; D008433:Mathematics; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins; D011485:Protein Binding; D012242:Rhodobacter sphaeroides / Q000378:metabolism*
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D045322:Photosynthetic Reaction Center Complex Proteins