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A vertebrate-type ferredoxin domain in the Na+-translocating NADH dehydrogenase from Vibrio cholerae
Mikrobiologisches Institut der Eidgenössischen Technischen Hochschule, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.ORCID iD: 0000-0002-9915-002x
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2005 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 280, no 24, p. 22560-22563Article in journal (Refereed) Published
Abstract [en]

The Na(+)-translocating NADH:quinone oxidoreductase from Vibrio cholerae contains a single Fe-S cluster localized in subunit NqrF. Here we study the electronic properties of the Fe-S center in a truncated version of the NqrF subunit comprising only its ferredoxin-like Fe-S domain. Mössbauer spectroscopy of the Fe-S domain in the oxidized state is consistent with a binuclear Fe-S cluster with tetrahedral sulfur coordination by the cysteine residues Cys(70), Cys(76), Cys(79), and Cys(111). Important sequence motifs surrounding these cysteines are conserved in the Fe-S domain and in vertebrate-type ferredoxins. The magnetic circular dichroism spectra of the photochemically reduced Fe-S domain exhibit a striking similarity to the magnetic circular dichroism spectra of vertebrate-type ferredoxins required for the in vivo assembly of iron-sulfur clusters. This study reveals a novel function for vertebrate-type [2Fe-2S] clusters as redox cofactors in respiratory dehydrogenases.

Place, publisher, year, edition, pages
2005. Vol. 280, no 24, p. 22560-22563
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Microbiology Biochemistry and Molecular Biology
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URN: urn:nbn:se:umu:diva-156953DOI: 10.1074/jbc.C500171200PubMedID: 15870079OAI: oai:DiVA.org:umu-156953DiVA, id: diva2:1293130
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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