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

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Description

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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Berry, Edward A. & Huang, Li-Shar September 7, 2003.

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Description

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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vp.

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  • Journal Name: Federation of European Biochemical Societies; Journal Volume: 555; Journal Issue: 1; Other Information: Journal Publication Date: 11/27/2003

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  • Report No.: LBNL--53853
  • Grant Number: AC03-76SF00098
  • Office of Scientific & Technical Information Report Number: 832755
  • Archival Resource Key: ark:/67531/metadc778645

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  • September 7, 2003

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  • Dec. 3, 2015, 9:30 a.m.

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  • June 22, 2016, 3:58 p.m.

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Berry, Edward A. & Huang, Li-Shar. Observations concerning the quinol oxidation site of the cytochrome bc{sub 1} complex, article, September 7, 2003; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc778645/: accessed August 20, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.