title: Biosynthesis of the metalloclusters of molybdenum nitrogenase.
abstract: Nitrogenase catalyzes a key step in the global nitrogen cycle, the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. There is a substantial amount of interest in elucidating the biosynthetic mechanisms of the FeMoco and the P-cluster of nitrogenase, because these clusters are not only biologically important but also chemically unprecedented. In this review, we summarize the recent advances in this research area, with an emphasis on our work that aims at providing structural and spectroscopic insights into the assembly of these complex metalloclusters.
authors: Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92687-3900, USA. yilinh@uci.edu
authors: Yilin
authors: Y
authors: Hu
authors: Markus W
authors: MW
authors: Ribbe
mesh_terms: D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism*; D008982:Molybdenum / Q000737:chemistry / Q000378:metabolism*; D009591:Nitrogenase / Q000737:chemistry / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000502:physiology
chemical_list: D008667:Metalloproteins; D008982:Molybdenum; D009591:Nitrogenase