Crystallization of Wolinella succinogenes quinol:fumarate reductase

Lancaster, C. Roy D.

doi:10.1016/B978-012361776-7/50014-0

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Crystallization of Wolinella succinogenes quinol:fumarate reductase

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Lancaster, C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Lancaster, C. R. D. (2003). Crystallization of Wolinella succinogenes quinol:fumarate reductase. In C. Hunte, G. von Jagow, & H. Schägger (Eds.), Membrane Protein Purification and Crystallization: A Practical Guide. (2nd edition, pp. 219-228). San Diego/USA: Academic Press Inc. doi:10.1016/B978-012361776-7/50014-0.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DB47-3

Abstract

INTRODUCTION
Quinol:fumarate reductases (QFR) and succinate:quinone reductases (SQR) catalyze the reduction of fumarate to succinate with concomitant oxidation of hydroquinone (quinol) to quinone, as well as the reverse reaction. SQR (respiratory complex II) is involved in aerobic metabolism as part of the citric acid cycle and the aerobic respiratory chain. QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor (Kröger, 1978; Kröger et al., 1992), and it is part of the electron transport chain catalyzing the oxidation of various donor substrates (e.g., NADH, H2 or formate) by fumarate. These reactions are coupled to ADP phosphorylation via an electrochemical proton potential.