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Literature summary extracted from

  • Juarez, O.; Nilges, M.J.; Gillespie, P.; Cotton, J.; Barquera, B.
    Riboflavin is an active redox cofactor in the Na+-pumping NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae (2008), J. Biol. Chem., 283, 33162-33167.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
7.2.1.1 S246A mutant that lacks the noncovalently bound FAD in NqrF Vibrio cholerae serotype O1
7.2.1.1 T236Y/T225Y NqrB-T236Y/NqrC-T225Y, double mutant that lacks both covalently bound FMN cofactors. The double mutant contains riboflavin and FAD in a 0.6:1 ratio, as the only flavins in the enzyme, noncovalently bound flavins are detected. In the oxidized form, the double mutant exhibits an EPR signal consistent with a neutral flavosemiquinone radical, which is abolished on reduction of the enzyme Vibrio cholerae serotype O1

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Vibrio cholerae serotype O1
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Synonyms

EC Number Synonyms Comment Organism
7.2.1.1 Na+-NQR
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 Vibrio cholerae serotype O1
7.2.1.1 Na+-pumping NADH:quinone oxidoreductase
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 Vibrio cholerae serotype O1

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 riboflavin riboflavin is an active redox cofactor of Na+-NQR, giving rise to the neutral flavosemiquinone, it is likely to be the final electron carrier in the enzyme before the quinone Vibrio cholerae serotype O1