Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins*
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Flavin-Adenine Dinucleotide
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Molecular Structure
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Protein Denaturation
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Quinone Reductases / analysis*
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Riboflavin / analogs & derivatives*
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Riboflavin / analysis*
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Sodium-Potassium-Exchanging ATPase*
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Vibrio cholerae / enzymology*
Substances
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Bacterial Proteins
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riboflavin 5'-phosphorothioate
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Flavin-Adenine Dinucleotide
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sodium-translocating NADH-quinone reductase
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Quinone Reductases
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Sodium-Potassium-Exchanging ATPase
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Riboflavin