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Originally published In Press as doi:10.1074/jbc.M004497200 on July 25, 2000

J. Biol. Chem., Vol. 275, Issue 41, 32277-32280, October 13, 2000
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MioC Is an FMN-binding Protein That Is Essential for Escherichia coli Biotin Synthase Activity in Vitro*

Olwen M. BirchDagger , Kirsty S. Hewitson§, Martin FuhrmannDagger , Knut BurgdorfDagger , Jack E. Baldwin§, Peter L. Roach||**, and Nicholas M. ShawDagger Dagger Dagger

From the Dagger  Biotechnology Research, Lonza A.G., CH-3930 Visp, Switzerland, § Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QY, United Kingdom, and the || Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom

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.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by the Biotechnology and Biological Sciences Research Council and Lonza U.K.

** Recipient of a Royal Society University Research Fellowship.

Dagger Dagger To whom correspondence should be addressed. Tel.: 41-279-485937; Fax: 41-279-475937; E-mail: nicholas.shaw@lonzagroup.com.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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