Multiphasic oxidation-reduction of cytochrome b in the succinate-cytochrome c reductase

The experimental data currently available suggest that QH2:cytochrome c oxidoreductase functions according to a Q-cycle type of mechanism. The molecular weight of the enzyme in a natural or artificial phospholipid bilayer or in solution corresponds to that of a dimer. The pre-steady state kinetics of reduction of the prosthetic groups indicate that the enzyme is functionally dimeric. A double Q cycle is proposed, describing the pathway of electron transfer in the dimeric QH2:cytochrome c oxidoreductase. According to this scheme, the two monomeric halves of the enzyme act in a cooperative fashion to complete the catalytic cycle. It is proposed that high-potential cytochrome b-562 and low-potential cytochrome b-562 act cooperatively, viz. as a functional pair, in the antimycin-sensitive reduction of ubiquinone to ubiquinol.

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Rapid redox equilibrium between the mitochondrial Q pool and cytochrome b during triphasic reduction of cytochrome b by succinate

Chen

Zhu

1986

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Multiphasic oxidation-reduction of cytochrome b in the succinate-cytochrome c reductase

Cited by 7 publications

References 23 publications

The Mechanism of the Ubiquinol: Cytochrome c Oxidoreductases of Mitochondria and of Rhodopseudomonas sphaeroides

The Mechanism of the Ubiquinol: Cytochrome c Oxidoreductases of Mitochondria and of Rhodopseudomonas sphaeroides

The pathway of electron transfer in the dimeric QH2: Cytochromec oxidoreductase

Rapid redox equilibrium between the mitochondrial Q pool and cytochrome b during triphasic reduction of cytochrome b by succinate

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