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

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
*
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.

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