Literature DB >> 10686111

A motif for quinone binding sites in respiratory and photosynthetic systems.

N Fisher1, P R Rich.   

Abstract

Many of the membrane-bound protein complexes of respiratory and photosynthetic systems are reactive with quinones. To date, no clear structural relationship between sites that bind quinone has been defined, apart from that in the homologous family of "type II" photosynthetic reaction centres. We show here that a structural element containing a weak sequence motif is common to the Q(A) and Q(B) sites of bacterial reaction centres and the Q(i) site of the mitochondrial bc(1) complex. Analyses of sequence databases indicate that this element may also be present in the PsaA/B subunits of photosystem I, in the ND4 and ND5 subunits of complex I and, possibly, in the mitochondrial alternative quinol oxidase. This represents a first step in the structural classification of quinone binding sites. Copyright 2000 Academic Press.

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Year:  2000        PMID: 10686111     DOI: 10.1006/jmbi.2000.3509

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  40 in total

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9.  The nature and mechanism of superoxide production by the electron transport chain: Its relevance to aging.

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10.  EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ.

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