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Observations concerning the quinol oxidation site of the cytochrome bc1 complex
Edward A Berry1, Li-shar Huang
1MS 64R121, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. eaberry@lbl.gov
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, electron paramagnetic resonance (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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