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Brian M. Hoffman,* Dmitriy Lukoyanov, Zhi-Yong Yang,† Dennis R. Dean,*,‡ and Lance C. Seefeldt*,† †Department of Chemistry and… Expand A central light atom in a cofactor at the nitrogenase active site is identified as a carbon. Nitrogenase is a complex enzyme that… Expand Nitrogen-fixing bacteria catalyze the reduction of dinitrogen (N(2)) to two ammonia molecules (NH(3)), the major contribution of… Expand Biological nitrogen fixation is an important source of fixed nitrogen for the biosphere. Microorganisms catalyse biological… Expand A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated… Expand Structural models for the nitrogenase FeMo-cofactor and P-clusters are proposed based on crystallographic analysis of the… Expand The nitrogenase enzyme system catalyzes the ATP (adenosine triphosphate)-dependent reduction of dinitrogen to ammonia during the… Expand The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined at 2.7… Expand The requirement for molybdenum in biological dinitrogen fixation, first reported by Bortels1, is due to its involvement at or… Expand A method for the isolation of an iron-molybdenum cofactor (FeMoCo) from component I of nitrogenase is described. This method is… Expand