Inactivation of the Na+‐translocating NADH:ubiquinone oxidoreductase from 
Vibrio alginolyticus by reactive oxygen species

Steuber, Julia; Rufibach, Michèle; Fritz, Günter; Neese, Frank; Dimroth, Peter

doi:10.1046/j.1432-1033.2002.02770.x

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Inactivation of the Na⁺‐translocating NADH:ubiquinone oxidoreductase from Vibrio alginolyticus by reactive oxygen species

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Steuber, J., Rufibach, M., Fritz, G., Neese, F., & Dimroth, P. (2002). Inactivation of the Na⁺‐translocating NADH:ubiquinone oxidoreductase from Vibrio alginolyticus by reactive oxygen species. European Journal of Biochemistry, 269(4), 1287-1292. doi:10.1046/j.1432-1033.2002.02770.x.

Cite as: https://hdl.handle.net/21.11116/0000-0007-F277-2

Abstract

The Na⁺‐translocating NADH:quinone oxidoreductase (Na⁺‐NQR) from Vibrio alginolyticus was inactivated by reactive oxygen species. Highest Na⁺‐NQR activity was observed in anaerobically prepared membranes that exhibited 1 : 1 coupling of NADH oxidation and Q reduction activities (1.6 U·mg⁻¹). Optical and EPR spectroscopy documented the presence of b‐type cytochromes, a [2Fe−2S] cluster and an organic radical signal in anaerobically prepared membranes from V. alginolyticus. It is shown that the [2Fe−2S] cluster previously assigned to the Na⁺‐NQR originates from the succinate dehydrogenase or the related enzyme fumarate reductase.