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Observations concerning the quinol oxidation site of the cytochrome bc{sub 1} complex

  • Author(s): Berry, Edward A.;
  • Huang, Li-Shar
  • et al.
Abstract

A direct hydrogen bond between ubiquinone/quinol bound at the QO site and a cluster-ligand histidine of the iron-sulfur protein (ISP) is described as a major determining factor explaining much experimental data on position of the ISP ectodomain, EPR lineshape and midpoint potential of the iron-sulfur cluster, and the mechanism of the bifurcated electron transfer from ubiquinol to the high and low potential chains of the bc1 complex.

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