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Article

The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b.

The Journal of biological chemistry - 27 Oct 2006

Tran Quang M, Rothery Richard A, Maklashina Elena, Cecchini Gary, Weiner Joel H

Abstract excerpt

We have examined the role of the quinone-binding (Q(P)) site of Escherichia coli succinate:ubiquinone oxidoreductase (succinate dehydrogenase) in heme reduction and reoxidation during enzyme turnover. The SdhCDAB electron transfer pathway leads from a cytosolically localized flavin adenine dinucleotide cofactor to a Q(P) site located within the membrane-intrinsic domain of the enzyme. The Q(P) site is sandwiched...

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Identifiers

PMID: 16950775
DOI: 10.1074/jbc.M607476200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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