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

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

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

@article{Casutt2011-11-18Local-21275, title={Localization of Ubiquinone-8 in the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae}, year={2011}, doi={10.1074/jbc.M111.224980}, 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 and Steuber, Julia} }

2011-11-18 eng Möller, Heiko deposit-license Gerken, Uwe Casutt, Marco S. Murai, Masatoshi Miyoshi, Hideto Miyoshi, Hideto Möller, Heiko Localization of Ubiquinone-8 in the Na<sup>+</sup>-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae Nedielkov, Ruslan 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. Murai, Masatoshi Wendelspiess, Severin Gerken, Uwe 2013-01-30T08:13:18Z Steuber, Julia Wendelspiess, Severin Nedielkov, Ruslan Vossler, Sara Journal of Biological Chemistry ; 286 (2011), 46. - S. 40075-40082 Steuber, Julia Casutt, Marco S. Vossler, Sara 2013-01-30T08:13:18Z

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