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J. Biol. Chem., Vol. 277, Issue 42, 40106-40111, October 18, 2002
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From the ¶ Department of Biochemistry and the
The biosynthesis of the iron-molybdenum cofactor
(FeMo-co) of nitrogenase was investigated using the purified in
vitro FeMo-co synthesis system and 99Mo. The purified
system involves the addition of all components that are known to be
required for FeMo-co synthesis in their purified forms. Here, we report
the accumulation of a 99Mo-containing FeMo-co precursor on
NifNE. Apart from NifNE, NifH and NifX also accumulate 99Mo
label. We present evidence that suggests NifH may serve as the entry
point for molybdenum incorporation into the FeMo-co biosynthetic
pathway. We also present evidence suggesting a role for NifX in
specifying the organic acid moiety of FeMo-co.
Accumulation of 99Mo-containing Iron-Molybdenum
Cofactor Precursors of Nitrogenase on NifNE, NifH, and NifX of
Azotobacter vinelandii*
§ and
¶
Center for the Study of Nitrogen Fixation, College of
Agricultural and Life Sciences, University of Wisconsin-Madison,
Madison, Wisconsin 53706
*
This work has been supported by National Institutes of
Health/NIGMS Grant GM35332 (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: College of Natural
Resources, University of California, Berkeley, 101 Giannini Hall, Rm.
3100, Berkeley, CA 94720. Tel.: 510-642-7171; Fax: 510-642-4612; E-mail: pludden@nature.berkeley.edu.
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