Asymmetric binding of stigmatellin to the dimeric Paracoccus denitrificans bc1 complex: evidence for anti-cooperative ubiquinol oxidation and communication between center P ubiquinol oxidation sites.

Abstract excerpt

We have investigated the mechanism responsible for half-of-the-sites activity in the dimeric cytochrome bc(1) complex from Paracoccus denitrificans by characterizing the kinetics of inhibitor binding to the ubiquinol oxidation site at center P. Both myxothiazol and stigmatellin induced a 2-3 nm shift of the visible absorbance spectrum of the b(L) heme. The shift generated by myxothiazol was symmetric, with...

Topics

• Binding Sites
• Dimerization
• Electron Transport Complex III
• Electrons
• Heme
• Hydrogen-Ion Concentration
• Kinetics
• Methacrylates
• Mutation
• Oxidation-Reduction