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  Experimental Evidence for Proton Motive Force-Dependent Catalysis by the Diheme-Containing Succinate:Menaquinone Oxidoreductase from the Gram-Positive Bacterium Bacillus licheniformis

Madej, M. G., Nasiri, H. R., Hilgendorff, N. S., Schwalbe, H., Unden, G., & Lancaster, C. R. D. (2006). Experimental Evidence for Proton Motive Force-Dependent Catalysis by the Diheme-Containing Succinate:Menaquinone Oxidoreductase from the Gram-Positive Bacterium Bacillus licheniformis. Biochemistry, 45(50), 15049-15055. doi:10.1021/bi0618161.

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Madej, M. Gregor1, Autor           
Nasiri, Hamid R.2, Autor
Hilgendorff, Nicole S.1, Autor           
Schwalbe, Harald2, Autor
Unden, Gottfried3, Autor
Lancaster, C. Roy D.1, Autor           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institut für Organische Chemie und Chemische Biologie, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-Universität, 60438 Frankfurt am Main, Germany, ou_persistent22              
3nstitut für Mikrobiologie und Weinforschung, Johannes Gutenberg-Universität Mainz, 55099 Mainz, Germany , ou_persistent22              

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Schlagwörter: Redox reactions; Quinones; Peptides and proteins; ,Bacteria; Oxidation
 Zusammenfassung: In Gram-positive bacteria and other prokaryotes containing succinate:menaquinone reductases, it has previously been shown that the succinate oxidase and succinate:menaquinone reductase activities are lost when the transmembrane electrochemical proton potential, Δp, is abolished by the rupture of the bacteria or by the addition of a protonophore. It has been proposed that the endergonic reduction of menaquinone by succinate is driven by the electrochemical proton potential. Opposite sides of the cytoplasmic membrane were envisaged to be separately involved in the binding of protons upon the reduction of menaquinone and their release upon succinate oxidation, with the two reactions linked by the transfer of two electrons through the enzyme. However, it has previously been argued that the observed Δp dependence is not associated specifically with the succinate:menaquinone reductase. Definitive insight into the mechanism of catalysis of this reaction requires a corresponding functional characterization of an isolated, membrane-bound succinate:menaquinone reductase from a Gram-positive bacterium. Here, we describe the purification, reconstitution into proteoliposomes, and functional characterization of the diheme-containing succinate:menaquinone reductase from the Gram-positive bacterium Bacillus licheniformis and, with the help of the design, synthesis, and characterization of quinones with finely tuned oxidation/reduction potentials, provide unequivocal evidence for Δp-dependent catalysis of succinate oxidation by quinone as well as for Δp generation upon catalysis of fumarate reduction by quinol.

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Sprache(n): eng - English
 Datum: 2006-10-052006-08-312006-11-232006-12-01
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1021/bi0618161
 Art des Abschluß: -

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Titel: Biochemistry
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Columbus, Ohio : American Chemical Society
Seiten: - Band / Heft: 45 (50) Artikelnummer: - Start- / Endseite: 15049 - 15055 Identifikator: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103