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  Limited reversibility of transmembrane proton transfer assisting transmembrane electron transfer in a dihaem-containing succinate:quinone oxidoreductase

Madej, M. G., Müller, F. G., Ploch, J., & Lancaster, C. R. D. (2009). Limited reversibility of transmembrane proton transfer assisting transmembrane electron transfer in a dihaem-containing succinate:quinone oxidoreductase. Biochimica et Biophysica Acta, Bioenergetics, 1787(6), 593-600. doi:10.1016/j.bbabio.2009.02.011.

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 Creators:
Madej, M. Gregor1, 2, Author           
Müller, Florian G.1, 2, Author           
Ploch, Julian1, 2, Author           
Lancaster, C. Roy D.1, 2, 3, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Cluster of Excellence “Macromolecular Complexes”, Max Planck Institute of Biophysics, Department of Molecular Membrane Biology, 60438 Frankfurt am Main, Germany, ou_persistent22              
3Saarland University, Department of Structural Biology, Faculty of Medicine, 66421 Homburg, Germany, ou_persistent22              

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Free keywords: Atomic model; Fumarate reductase; Membrane protein; Transmembrane electrochemical proton potential; Transmembrane electron transfer; Transmembrane proton transfer
 Abstract: Membrane protein complexes can support both the generation and utilisation of a transmembrane electrochemical proton potential (Δp), either by supporting transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by supporting transmembrane proton transfer. The first mechanism has been unequivocally demonstrated to be operational for Δp-dependent catalysis of succinate oxidation by quinone in the case of the dihaem-containing succinate:menaquinone reductase (SQR) from the Gram-positive bacterium Bacillus licheniformis. This is physiologically relevant in that it allows the transmembrane potential Δp to drive the endergonic oxidation of succinate by menaquinone by the dihaem-containing SQR of Gram-positive bacteria. In the case of a related but different respiratory membrane protein complex, the dihaem-containing quinol:fumarate reductase (QFR) of the ɛ-proteobacterium Wolinella succinogenes, evidence has been obtained that both mechanisms are combined, so as to facilitate transmembrane electron transfer by proton transfer via a both novel and essential compensatory transmembrane proton transfer pathway (“E-pathway”). Although the reduction of fumarate by menaquinol is exergonic, it is obviously not exergonic enough to support the generation of a Δp. This compensatory “Epathway” appears to be required by all dihaem-containing QFR enzymes and results in the overall reaction being electroneutral. However, here we show that the reverse reaction, the oxidation of succinate by quinone, as catalysed by W. succinogenes QFR, is not electroneutral. The implications for transmembrane proton transfer via the E-pathway are discussed

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Language(s): eng - English
 Dates: 2009-02-172008-12-222009-02-182009-02-272009-06
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbabio.2009.02.011
 Degree: -

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1787 (6) Sequence Number: - Start / End Page: 593 - 600 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6

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Title: Biochimica et Biophysica Acta (BBA) - Bioenergetics
  Alternative Title : Biochim. Biophys. Acta
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 1787 (6) Sequence Number: - Start / End Page: - Identifier: -