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Defining a direction: Electron transfer and catalysis in Escherichia coli complex II enzymes

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1827, Issue 5, Pages 668-678

Publisher

ELSEVIER
DOI: 10.1016/j.bbabio.2013.01.010

Keywords

Complex II; Succinate:quinone oxidoreductase; Quinol:fumarate reductase; Protein electron transport; Iron sulfur cluster; Quinone binding site

Funding

  1. Department of Veterans Affairs, Biomedical Laboratory Research and Development
  2. National Institutes of Health [GM61606, GM62954]
  3. Chemical Sciences, Geosciences and Biosciences Division, Office of Basic Energy Sciences, Office of Sciences, U.S. Department of Energy [DE-FG02-08ER15960]

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There are two homologous membrane-bound enzymes in Escherichia coli that catalyze reversible conversion between succinate/fumarate and quinone/quinol. Succinate:ubiquinone reductase (SQR) is a component of aerobic respiratory chains, whereas quinol:fumarate reductase (QFR) utilizes menaquinol to reduce fumarate in a final step of anaerobic respiration. Although, both protein complexes are capable of supporting bacterial growth on either minimal succinate or fumarate media, the enzymes are more proficient in their physiological directions. Here we evaluate factors that may underlie this catalytic bias. This article is part of a Special Issue entitled: Respiratory complex II: Role in cellular physiology and disease. (C) 2013 Elsevier B.V. All rights reserved.

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