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J Biol Chem, Vol. 274, Issue 41, 29413-29419, October 8, 1999

Inhibition of Iron-Molybdenum Cofactor Biosynthesis by L127 NifH and Evidence for a Complex Formation between L127 NifH and NifNE

Priya Rangaraj, Matthew J. Ryle, William N. Lanzilotta, Paul J. Goodwin^¶, Dennis R. Dean^¶, Vinod K. Shah, and Paul W. Ludden

From the Department of Biochemistry and Center for the Study of Nitrogen Fixation, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706,  Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, and ^¶ Department of Biochemistry, Fralin Biotechnology Center, Virginia Tech, Blacksburg, Virginia 24061

Besides serving as the obligate electron donor to dinitrogenase during nitrogenase turnover, dinitrogenase reductase (NifH) is required for the biosynthesis of the iron-molybdenum cofactor (FeMo-co) and for the maturation of ₂₂ apo-dinitrogenase (apo-dinitrogenase maturation). In an attempt to understand the role of NifH in FeMo-co biosynthesis, a site-specific altered form of NifH in which leucine at position 127 has been deleted, L127, was employed in in vitro FeMo-co synthesis assays. This altered form of NifH has been shown to inhibit substrate reduction by the wild-type nitrogenase complex, forming a tight protein complex with dinitrogenase. The L127 NifH was found to inhibit in vitro FeMo-co synthesis by wild-type NifH as detected by the  gel shift assay. Increasing the concentration of NifNE and NifB-cofactor (NifB-co) relieved the inhibition of FeMo-co synthesis by L127 NifH. The formation of a complex of L127 NifH with NifNE was investigated by gel filtration chromatography. We herein report the formation of a complex between L127 NifH and NifNE in the presence of NifB-co. This work presents evidence for one of the possible roles for NifH in FeMo-co biosynthesis, i.e. the interaction of NifH with a NifNE·NifB-co complex.

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