Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase (Q27696310)

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Georg Vohl

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Marco S Casutt

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Thomas Vorburger

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Günter Fritz

Dali server: conservation mapping in 3D

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language of work or name

English

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publication date

4 December 2014

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published in

Nature

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volume

516

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issue

7529

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page(s)

62-7

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cites work

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NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae

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Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae.

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Redox properties of the prosthetic groups of Na(+)-translocating nadh:quinone oxidoreductase. 1. Electron paramagnetic resonance study of the enzyme

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The Na+/e- stoichiometry of the Na+-motive NADH:quinone oxidoreductase in Vibrio alginolyticus

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PubMed

https://pubmed.ncbi.nlm.nih.gov/25471880

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

The single NqrB and NqrC subunits in the Na(+)-translocating NADH: quinone oxidoreductase (Na(+)-NQR) from Vibrio cholerae each carry one covalently attached FMN

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/25471880