title: Nitrogenase: standing at the crossroads.
abstract: Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia, which is central to the process of biological nitrogen fixation. Recent progress towards establishing the mechanism of action of this complex metalloenzyme reflects the contributions of a combination of structural, biochemical, spectroscopic, synthetic and theoretical approaches to a challenging problem with implications for a range of biochemical and chemical systems.
authors.affiliation: Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA. dcrees@caltech.edu
authors.forename: D C
authors.initials: DC
authors.lastname: Rees
authors.forename: J B
authors.initials: JB
authors.lastname: Howard
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D002384:Catalysis; D007700:Kinetics; D009591:Nitrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction
chemical_list: D000255:Adenosine Triphosphate; D009591:Nitrogenase