Literature summary for 7.2.1.1 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.

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Protein Variants

Protein Variants	Comment	Organism
S246A	mutant that lacks the noncovalently bound FAD in NqrF	Vibrio cholerae serotype O1
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

Organism	UniProt	Comment	Textmining
Vibrio cholerae serotype O1	-	-	-

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
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

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Release 2023.1 (January 2023)