Riboflavin is a component of the Na+-pumping NADH-quinone oxidoreductase from Vibrio cholerae.
Flavins are cofactors in many electron-transfer enzymes. Typically, two types of flavins perform this role: 5'-phosphoriboflavin (FMN) and flavin-adenine dinucleotide (FAD). Both of these are riboflavin derivatives, but riboflavin itself has never been reported to be an enzyme-bound component. We now report that tightly bound riboflavin is a component of the NADH-driven sodium pump from Vibrio cholerae.
Barquera
Blanca
B
Department of Biochemistry, University of Illinois, 600 South Mathews Street, Urbana, IL 61801, USA.
Zhou
Weidong
W
Morgan
Joel E
JE
Gennis
Robert B
RB
D001426:Bacterial Proteins; D005182:Flavin-Adenine Dinucleotide; D015394:Molecular Structure; D011489:Protein Denaturation; D011808:Quinone Reductases / Q000032:analysis*; D012256:Riboflavin / Q000031:analogs & derivatives* / Q000032:analysis*; D000254:Sodium-Potassium-Exchanging ATPase; D014734:Vibrio cholerae / Q000201:enzymology*
D001426:Bacterial Proteins; C054180:riboflavin 5'-phosphorothioate; D005182:Flavin-Adenine Dinucleotide; C084142:sodium-translocating NADH-quinone reductase; D011808:Quinone Reductases; D000254:Sodium-Potassium-Exchanging ATPase; D012256:Riboflavin