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J Biol Chem, Vol. 274, Issue 22, 15869-15874, May 28, 1999

Incorporation of Molybdenum into the Iron-Molybdenum Cofactor of Nitrogenase

Ronda M. Allen^§, Jon T. Roll^§, Priya Rangaraj^§, Vinod K. Shah^§, Gary P. Roberts^§, and Paul W. Ludden^§

From the Departments of  Biochemistry and  Bacteriology and the ^§ Center for the Study of Nitrogen Fixation, University of Wisconsin, Madison, Wisconsin 53706

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.

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