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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Binding Sites
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Cattle
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Crystallography, X-Ray
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Electron Spin Resonance Spectroscopy
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Electron Transport
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Electron Transport Complex III / antagonists & inhibitors
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Electron Transport Complex III / chemistry*
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Electron Transport Complex III / metabolism
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Histidine / chemistry
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Hydrogen Bonding
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Hydroquinones / chemistry
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In Vitro Techniques
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Models, Molecular
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Oxidation-Reduction
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Protein Conformation
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Static Electricity
Substances
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Hydroquinones
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Histidine
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Electron Transport Complex III