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  A Vertebrate-type Ferredoxin Domain in the Na+-translocating NADH Dehydrogenase from Vibrio cholerae

Lin, P.-C., Puhar, A., Türk, K., Piligkos, S., Bill, E., Neese, F., et al. (2005). A Vertebrate-type Ferredoxin Domain in the Na+-translocating NADH Dehydrogenase from Vibrio cholerae. The Journal of Biological Chemistry, 280(24), 22560-22563. doi:10.1074/jbc.C500171200.

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 Creators:
Lin, Po-Chi1, Author
Puhar, Andrea1, Author
Türk, Karin1, Author
Piligkos, Stergios2, Author              
Bill, Eckhard2, Author              
Neese, Frank2, Author              
Steuber, Julia1, Author
Affiliations:
1Mikrobiologisches Institut der Eidgenössischen Technischen Hochschule, ETH-Hönggerberg, CH-8093 Zürich, Switzerland, ou_persistent22              
2Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society, ou_3023881              

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 Abstract: 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 Cys70, Cys76, Cys79, and Cys111. 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.

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Language(s): eng - English
 Dates: 2005-04-182005-06-17
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.C500171200
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
  Abbreviation : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 280 (24) Sequence Number: - Start / End Page: 22560 - 22563 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1