@article{Steuber2014Struc-29488,
  year={2014},
  doi={10.1038/nature14003},
  title={Structure of the V. cholerae Na<sup>+</sup>-pumping NADH:quinone oxidoreductase},
  number={7529},
  volume={516},
  issn={0028-0836},
  journal={Nature},
  pages={62--67},
  author={Steuber, Julia and Vohl, Georg and Casutt, Marco S. and Diederichs, Kay and Fritz, Günter}
}

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    <dc:contributor>Vohl, Georg</dc:contributor>
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    <dc:contributor>Steuber, Julia</dc:contributor>
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    <dc:creator>Fritz, Günter</dc:creator>
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    <dc:contributor>Casutt, Marco S.</dc:contributor>
    <dc:creator>Vohl, Georg</dc:creator>
    <dc:rights>terms-of-use</dc:rights>
    <dc:creator>Casutt, Marco S.</dc:creator>
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    <dcterms:title>Structure of the V. cholerae Na&lt;sup&gt;+&lt;/sup&gt;-pumping NADH:quinone oxidoreductase</dcterms:title>
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    <dcterms:abstract xml:lang="eng">NADH oxidation in the respiratory chain is coupled to ion translocation across the membrane to build up an electrochemical gradient. The sodium-translocating NADH:quinone oxidoreductase (Na&lt;sup&gt;+&lt;/sup&gt;-NQR), a membrane protein complex widespread among pathogenic bacteria, consists of six subunits, NqrA, B, C, D, E and F. To our knowledge, no structural information on the Na&lt;sup&gt;+&lt;/sup&gt;-NQR complex has been available until now. Here we present the crystal structure of the Na&lt;sup&gt;+&lt;/sup&gt;-NQR complex at 3.5 Å resolution. The arrangement of cofactors both at the cytoplasmic and the periplasmic side of the complex, together with a hitherto unknown iron centre in the midst of the membrane-embedded part, reveals an electron transfer pathway from the NADH-oxidizing cytoplasmic NqrF subunit across the membrane to the periplasmic NqrC, and back to the quinone reduction site on NqrA located in the cytoplasm. A sodium channel was localized in subunit NqrB, which represents the largest membrane subunit of the Na&lt;sup&gt;+&lt;/sup&gt;-NQR and is structurally related to urea and ammonia transporters. On the basis of the structure we propose a mechanism of redox-driven Na&lt;sup&gt;+&lt;/sup&gt; translocation where the change in redox state of the flavin mononucleotide cofactor in NqrB triggers the transport of Na&lt;sup&gt;+&lt;/sup&gt; through the observed channel.</dcterms:abstract>
    <dc:contributor>Fritz, Günter</dc:contributor>
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