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

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Piligkos,  Stergios
Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Bill,  Eckhard
Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Neese,  Frank
Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0008-36B7-D
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.