Recent advances in cytochrome bc1: Inter monomer electronic communication?

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Title
Recent advances in cytochrome bc1: Inter monomer electronic communication?
Author(s)
B Khalfaoui-Hassani; P Lanciano; Dong-Woo Lee; E Darrouzet; F Daldal
Bibliographic Citation
FEBS Letters, vol. 586, no. 5, pp. 617-621
Publication Year
2012
Abstract
The ubihydroquinone: cytochrome c oxidoreductase, or cytochrome bc 1, is a central component of photosynthetic and respiratory energy transduction pathways in many organisms. It contributes to the generation of membrane potential and proton gradient used for cellular energy production (ATP). The three-dimensional structures of cytochrome bc 1 indicate that its two monomers are intertwined to form a symmetrical homodimer. This unusual architecture raises the issue of whether the monomers operate independently, or function cooperatively during the catalytic cycle of the enzyme. In this review, recent progresses achieved in our understanding of the mechanism of function of dimeric cytochrome bc 1 are presented. New genetic approaches producing heterodimeric enzymes, and emerging insights related to the inter monomer electron transfer between the heme b cofactors of cytochrome bc 1 are described.
Keyword
Inter monomer electron transferQ cycle mechanismRhodobacter capsulatusCytochrome bc 1Heterodimer
ISSN
0014-5793
Publisher
Wiley
DOI
http://dx.doi.org/10.1016/j.febslet.2011.08.032
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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