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  Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism [Review]

Kröger, A., Biel, S., Simon, J., Gross, R., Unden, G., & Lancaster, C. R. D. (2002). Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism [Review]. Biochimica et Biophysica Acta, Bioenergetics, 1553(1-2), 23-38. doi:10.1016/S0005-2728(01)00234-1.

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 Creators:
Kröger, Achim1, Author
Biel, Simone1, Author
Simon, Jörg1, Author
Gross, Roland1, Author
Unden, Gottfried1, Author
Lancaster, C. Roy D.2, Author           
Affiliations:
1Institut für Mikrobiologie, Johann Wolfgang Goethe-Universität, 60439 Frankfurt am Main, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Fumarate respiration; Electron transport; Coupling mechanism; Hydrogenase; Formate dehydrogenase; Wolinella succinogenes; Phosphorylative electron-transport; Bacillus-subtilis succinate; Cytochrome-c-oxidase; Vibrio-succinogenes; Atp synthase; Quinone oxidoreductases; Menaquinone reduction; Desulfovibrio-gigas; Crystal-structure; Reductase
 Abstract: Wolinella succinogenes performs oxidative phosphorylation with fumarate instead of O2 as terminal electron acceptor and H2 or formate as electron donors. Fumarate reduction by these donors ('fumarate respiration') is catalyzed by an electron transport chain in the bacterial membrane, and is coupled to the generation of an electrochemical proton potential (Deltap) across the bacterial membrane. The experimental evidence concerning the electron transport and its coupling to Deltap generation is reviewed in this article. The electron transport chain consists of fumarate reductase, menaquinone (MK) and either hydrogenase or formate dehydrogenase. Measurements indicate that the Deltap is generated exclusively by MK reduction with H-2 or formate; MKH2 oxidation by fumarate appears to be an electroneutral process. However, evidence derived from the crystal structure of fumarate reductase suggests an electrogenic mechanism for the latter process. (C) 2002 Elsevier Science B.V. All rights reserved. [References: 67]

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Language(s): eng - English
 Dates: 2001-08-272001-05-102001-10-122001-11-302002-01-17
 Publication Status: Issued
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0005-2728(01)00234-1
 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: 1553 (1-2) Sequence Number: - Start / End Page: 23 - 38 Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6