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Biochim Biophys Acta. 2010 Dec;1797(12):1910-6. doi: 10.1016/j.bbabio.2010.10.007. Epub 2010 Oct 16.

The electron transfer flavoprotein: ubiquinone oxidoreductases.

Author information

1
Centre for Molecular Structure and Biochemistry, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK. n.watmough@uea.ac.uk

Abstract

Electron transfer flavoprotein: ubiqionone oxidoreductase (ETF-QO) is a component of the mitochondrial respiratory chain that together with electron transfer flavoprotein (ETF) forms a short pathway that transfers electrons from 11 different mitochondrial flavoprotein dehydrogenases to the ubiquinone pool. The X-ray structure of the pig liver enzyme has been solved in the presence and absence of a bound ubiquinone. This structure reveals ETF-QO to be a monotopic membrane protein with the cofactors, FAD and a [4Fe-4S](+1+2) cluster, organised to suggests that it is the flavin that serves as the immediate reductant of ubiquinone. ETF-QO is very highly conserved in evolution and the recombinant enzyme from the bacterium Rhodobacter sphaeroides has allowed the mutational analysis of a number of residues that the structure suggested are involved in modulating the reduction potential of the cofactors. These experiments, together with the spectroscopic measurement of the distances between the cofactors in solution have confirmed the intramolecular pathway of electron transfer from ETF to ubiquinone. This approach can be extended as the R. sphaeroides ETF-QO provides a template for investigating the mechanistic consequences of single amino acid substitutions of conserved residues that are associated with a mild and late onset variant of the metabolic disease multiple acyl-CoA dehydrogenase deficiency (MADD).

PMID:
20937244
DOI:
10.1016/j.bbabio.2010.10.007
[Indexed for MEDLINE]
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