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NADH oxidation by the Na+-translocating NADH: quinone oxidoreductase from Vibrio cholerae
Mikrobiologisches Institut der Eidgenössischen Technischen Hochschule, ETH-Zentrum, CH-8092 Zürich, Switzerland.ORCID iD: 0000-0002-9915-002x
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2004 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 279, no 20, p. 21349-21355Article in journal (Refereed) Published
Abstract [en]

The Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae is a six subunit enzyme containing four flavins and a single motif for the binding of a Fe-S cluster on its NqrF subunit. This study reports the production of a soluble variant of NqrF (NqrF') and its individual flavin and Fe-S-carrying domains using V. cholerae or Escherichia coli as expression hosts. NqrF' and the flavin domain each contain 1 mol of FAD/mol of enzyme and exhibit high NADH oxidation activity (20,000 micromol min(-1) mg(-1)). EPR, visible absorption, and circular dichroism spectroscopy indicate that the Fe-S cluster in NqrF' and its Fe-S domain is related to 2Fe ferredoxins of the vertebrate-type. The addition of NADH to NqrF' results in the formation of a neutral flavosemiquinone and a partial reduction of the Fe-S cluster. The NqrF subunit harbors the active site of NADH oxidation and acts as a converter between the hydride donor NADH and subsequent one-electron reaction steps in the Na(+)-translocating NADH:quinone oxidoreductase complex. The observed electron transfer NADH --> FAD --> [2Fe-2S] in NqrF requires positioning of the FAD and the Fe-S cluster in close proximity in accordance with a structural model of the subunit.

Place, publisher, year, edition, pages
2004. Vol. 279, no 20, p. 21349-21355
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Natural Sciences Biological Sciences Microbiology Biochemistry and Molecular Biology
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URN: urn:nbn:se:umu:diva-156955DOI: 10.1074/jbc.M311692200PubMedID: 15010474OAI: oai:DiVA.org:umu-156955DiVA, id: diva2:1293132
Available from: 2019-03-03 Created: 2019-03-03 Last updated: 2019-03-11Bibliographically approved

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Puhar, Andrea

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