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J. Biol. Chem., Vol. 276, Issue 19, 15968-15974, May 11, 2001
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From the Department of Biochemistry and Center for the Study of
Nitrogen Fixation, College of Agricultural and Life Sciences,
University of Wisconsin-Madison, Madison, Wisconsin 53706
Iron-molybdenum cofactor (FeMo-co) biosynthesis
involves the participation of several proteins. We have used
55Fe-labeled NifB-co, the specific iron and
sulfur donor to FeMo-co, to investigate the accumulation of
protein-bound precursors of FeMo-co. The 55Fe label from
radiolabeled NifB-co became associated with two major protein bands
when the in vitro FeMo-co synthesis reaction was carried
out with the extract of an Azotobacter vinelandii mutant
lacking apodinitrogenase. One of the bands, termed
55Fe-labeled upper band, was purified and shown to be NifH
by immunoblot analysis. The 55Fe-labeled lower band was
identified as NifX by N-terminal sequencing. NifX purified from an
A. vinelandii nifB strain showed a different electrophoretic mobility on anoxic native gels than did NifX with the
FeMo-co precursor bound.
Accumulation of 55Fe-Labeled Precursors of the
Iron-Molybdenum Cofactor of Nitrogenase on NifH and NifX of
Azotobacter vinelandii*
*
This work was supported by NIGMS, National Institutes of
Health Grant 35332 (to P. W. L.).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: Department of
Biochemistry, 433 Babcock Ave., University of Wisconsin-Madison, Madison, WI 53706. Tel.: 608-262-6859; Fax: 608-262-3453; E-mail: ludden@biochem.wisc.edu.
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