| Literature DB >> 14630312 |
Edward A Berry1, Li-shar Huang.
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.Entities:
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Year: 2003 PMID: 14630312 DOI: 10.1016/s0014-5793(03)01099-8
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124