@article{Casutt2011-11-18Local-21275,
  year={2011},
  doi={10.1074/jbc.M111.224980},
  title={Localization of Ubiquinone-8 in the Na<sup>+</sup>-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae},
  number={46},
  volume={286},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={40075--40082},
  author={Casutt, Marco S. and Nedielkov, Ruslan and Wendelspiess, Severin and Vossler, Sara and Gerken, Uwe and Murai, Masatoshi and Miyoshi, Hideto and Möller, Heiko M. and Steuber, Julia}
}

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    <dc:contributor>Nedielkov, Ruslan</dc:contributor>
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    <dc:contributor>Miyoshi, Hideto</dc:contributor>
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    <dc:creator>Gerken, Uwe</dc:creator>
    <dc:creator>Wendelspiess, Severin</dc:creator>
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    <dc:contributor>Murai, Masatoshi</dc:contributor>
    <dc:contributor>Vossler, Sara</dc:contributor>
    <dc:contributor>Möller, Heiko M.</dc:contributor>
    <dc:contributor>Gerken, Uwe</dc:contributor>
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    <dc:contributor>Wendelspiess, Severin</dc:contributor>
    <dc:creator>Möller, Heiko M.</dc:creator>
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    <dcterms:abstract xml:lang="eng">Na + is the second major coupling ion at membranes after protons, and many pathogenic bacteria use the sodium-motive force to their advantage. A prominent example is Vibrio cholerae, which relies on the Na+ -pumping NADH:quinone oxidoreductase (Na + -NQR) as the first complex in its respiratory chain. The Na + -NQR is a multisubunit, membrane-embedded NADH dehydrogenase that oxidizes NADH and reduces quinone to quinol. Existing models describing redox-driven Na + translocation by the Na + -NQR are based on the assumption that the pump contains four flavins and one FeS cluster. Here we show that the large, peripheral NqrA subunit of the Na + -NQR binds one molecule of ubiquinone-So Investigations of the dynamic interaction of NqrA with quinones by surface plasmon resonance and saturation transfer difference NMR reveal a high affinity, which is determined by the methoxy groups at the C-2 and C-3 positions of the quinone headgroup. Using photoactivatable quinone derivatives, it is demonstrated that ubiquinone-S bound to NqrA occupies a functional site. A novel scheme of electron transfer in Na + -NQR is proposed that is initiated by NADH oxidation on sub unit NqrF and leads to quinol formation on subunit NqrA.</dcterms:abstract>
    <dcterms:issued>2011-11-18</dcterms:issued>
    <dc:creator>Casutt, Marco S.</dc:creator>
    <dc:creator>Murai, Masatoshi</dc:creator>
    <dcterms:title>Localization of Ubiquinone-8 in the Na&lt;sup&gt;+&lt;/sup&gt;-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae</dcterms:title>
    <dc:contributor>Casutt, Marco S.</dc:contributor>
    <dc:contributor>Steuber, Julia</dc:contributor>
    <dcterms:bibliographicCitation>Journal of Biological Chemistry ; 286 (2011), 46. - S. 40075-40082</dcterms:bibliographicCitation>
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    <dc:creator>Miyoshi, Hideto</dc:creator>
    <dc:language>eng</dc:language>
    <dc:creator>Vossler, Sara</dc:creator>
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