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  • Title: The nature and magnitude of the charge-separation reactions of ubiquinol cytochrome c2 oxidoreductase.
    Author: Robertson DE, Dutton PL.
    Journal: Biochim Biophys Acta; 1988 Oct 05; 935(3):273-91. PubMed ID: 2844257.
    Abstract:
    The transdielectric charge separation reaction catalyzed by the ubiquinol-cytochrome c2 oxidoreductase is achieved in two fractional steps. We present a detailed analysis which addresses the nature of the charge transferred, the redox groups directly involved in charge separation and the contributions of each to the full charge separation catalyzed by the enzyme. Accounting for light saturation effects, reaction centers unconnected to cytochrome c2 and the fraction of total cytochrome bc1 turning over per flash permits detailed quantitation of: (1) the red carotenoid bandshift associated with electron transfer between ubiquinol at site Qz and the high- (2Fe2S center, cytochrome c1) and low-potential (cytochrome bL, cytochrome bH) components of cytochrome bc1; (2) the blue bandshift accompanying reduction of cytochrome bH by ubiquinol via site Qc (the reverse of the physiological reaction); and (3) the effect of delta psi on the Qc-cytochrome bH redox equilibrium. Studies were performed at pH values above and below the redox-linked pK values of the redox centers known to be involved in each reaction at equilibrium. The conclusions of this study may be summarized as follows: (1) there is no transdielectric charge separation apparent in the redox reactions between Qz and cytochrome bL, 2Fe2S and cytochrome c1 (in agreement with Glaser, E. and Crofts, A.R. (1984) Biochim. Biophys. Acta 766, 223-235), i.e., charge separation accompanies electron transfer between cytochrome bL and cytochrome bH; (2) the redox reactions between cytochrome bL and cytochrome bH and between cytochrome bH and Qc constitute the full electrogenic span; (3) electron transfer between cytochrome bL and cytochrome bH contributes approx. 60% of this span; (4) electron transfer between cytochrome bH and Qc contributes 45-55% as calculated from the blue bandshift or the delta psi-dependent equilibrium shift; (5) there is no discernable pH dependence of the Qz-cytochrome bH or Qc-cytochrome bH charge-separation reactions; (6) cytochrome bL, Qz, 2Fe2S, and cytochrome c1 are on the periplasmic side out of the low dielectric part of the membrane while cytochrome bH is buried in the low dielectric medium; (7) electron transfer is the predominant if not the sole contributor to charge separation; (8) Qz and Qc are on opposite sides of the membrane dielectric profile.
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