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J Biol Chem, Vol. 274, Issue 22, 15869-15874, May 28, 1999
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From the Departments of The biosynthesis of the iron-molybdenum cofactor
(FeMo-co) of dinitrogenase was investigated using
99Mo to follow the incorporation of Mo into
precursors. 99Mo label accumulates on dinitrogenase only
when all known components of the FeMo-co synthesis system, NifH, NifNE,
NifB-cofactor, homocitrate, MgATP, and reductant, are present.
Furthermore, 99Mo label accumulates only on the gamma
protein, which has been shown to serve as a chaperone/insertase for the
maturation of apodinitrogenase when all known components are present.
It appears that only completed FeMo-co can accumulate on the gamma
protein. Very little FeMo-co synthesis was observed when all known
components are used in purified forms, indicating that additional
factors are required for optimal FeMo-co synthesis. 99Mo
did not accumulate on NifNE under any conditions tested, suggesting that Mo enters the pathway at some other step, although it remains possible that a Mo-containing precursor of FeMo-co that is not sufficiently stable to persist during gel electrophoresis occurs but is
not observed. 99Mo accumulates on several unidentified
species, which may be the additional components required for FeMo-co
synthesis. The molybdenum storage protein was observed and the
accumulation of 99Mo on this protein required nucleotide.
Biochemistry and
Bacteriology and the § Center for the Study of
Nitrogen Fixation, University of Wisconsin,
Madison, Wisconsin 53706
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