MioC Is an FMN-binding Protein That Is Essential forEscherichia coli Biotin Synthase Activity in Vitro

Biotin synthase is required for the conversion of dethiobiotin to biotin and requires a number of accessory proteins and small molecule cofactors for activity in vitro. We have previously identified two of these proteins as flavodoxin and ferredoxin (flavodoxin) NADP+ reductase. We now report the id...

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Published inThe Journal of biological chemistry Vol. 275; no. 41; pp. 32277 - 32280
Main Authors Birch, Olwen M., Hewitson, Kirsty S., Fuhrmann, Martin, Burgdorf, Knut, Baldwin, Jack E., Roach, Peter L., Shaw, Nicholas M.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 13.10.2000
American Society for Biochemistry and Molecular Biology
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Summary:Biotin synthase is required for the conversion of dethiobiotin to biotin and requires a number of accessory proteins and small molecule cofactors for activity in vitro. We have previously identified two of these proteins as flavodoxin and ferredoxin (flavodoxin) NADP+ reductase. We now report the identification of MioC as a third essential protein, together with its cloning, purification, and characterization. Purified MioC has a UV-visible spectrum characteristic of a flavoprotein and contains flavin mononucleotide. The presence of flavin mononucleotide and the primary sequence similarity to flavodoxin suggest that MioC may function as an electron transport protein. The role of MioC in the biotin synthase reaction is discussed, and the structure and function of MioC is compared with that of flavodoxin.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M004497200