Localization of Ubiquinone-8 in the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae

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2011
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Casutt, Marco S.
Wendelspiess, Severin
Vossler, Sara
Gerken, Uwe
Murai, Masatoshi
Miyoshi, Hideto
Steuber, Julia
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Journal of Biological Chemistry. 2011, 286(46), pp. 40075-40082. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M111.224980
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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.

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ISO 690CASUTT, Marco S., Ruslan NEDIELKOV, Severin WENDELSPIESS, Sara VOSSLER, Uwe GERKEN, Masatoshi MURAI, Hideto MIYOSHI, Heiko M. MÖLLER, Julia STEUBER, 2011. Localization of Ubiquinone-8 in the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae. In: Journal of Biological Chemistry. 2011, 286(46), pp. 40075-40082. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M111.224980
BibTex
@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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    <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>
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