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Identification of the binding sites for ubiquinone and inhibitors in the Na⁺-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae by photoaffinity labeling.

ABSTRACT: The Na⁺-pumping NADH-quinone oxidoreductase (Na⁺-NQR) is the first enzyme of the respiratory chain and the main ion transporter in many marine and pathogenic bacteria, including Vibrio cholerae The V. cholerae Na⁺-NQR has been extensively studied, but its binding sites for ubiquinone and inhibitors remain controversial. Here, using a photoreactive ubiquinone PUQ-3 as well as two aurachin-type inhibitors [¹²⁵I]PAD-1 and [¹²⁵I]PAD-2 and photoaffinity labeling experiments on the isolated enzyme, we demonstrate that the ubiquinone ring binds to the NqrA subunit in the regions Leu-32-Met-39 and Phe-131-Lys-138, encompassing the rear wall of a predicted ubiquinone-binding cavity. The quinolone ring and alkyl side chain of aurac

SUBMITTER: Ito T

PROVIDER: S-EPMC5427254 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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Identification of the binding sites for ubiquinone and inhibitors in the Na⁺-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae by photoaffinity labeling.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Identification of the binding sites for ubiquinone and inhibitors in the Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae by photoaffinity labeling.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Identification of the binding sites for ubiquinone and inhibitors in the Na⁺-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae by photoaffinity labeling.