title: Thermodynamics of the mechanism of the nitrogenase reaction.
abstract: The fixation of molecular nitrogen by nitrogenase requires a lot of energy because 16 mol of ATP are hydrolyzed per mole of nitrogen converted to ammonia. Kim and Dees determined the crystallograpic structure of nitrogenase and this has led to a three-step mechanism that involves Feprotein and MoFeprotein in addition to ferredoxin. Each of these steps can be interpreted in terms of two half reactions that are connected through their transfer of electrons. Estimates can be made of the standard apparent reduction potentials of these three steps and their dependencies on pH and ionic strength. This mechanism is compared with the same type of analysis of an alternative three-step mechanism in which the hydrolysis of ATP is coupled with the reduction of molecular nitrogen, rather than the reduction of Feprotein. The problem with the first mechanism is that the second step produces 12 mol of hydrogen ions per mole of nitrogen fixed and the third step consumes 10 mol of hydrogen ions per mole of nitrogen fixed. The alternative mechanism does not have this problem.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Cambridge, 02139, USA. alberty@mit.edu
authors.forename: Robert A
authors.initials: RA
authors.lastname: Alberty
mesh_terms: D008956:Models, Chemical; D009584:Nitrogen / Q000737:chemistry / Q000378:metabolism*; D009591:Nitrogenase / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D009591:Nitrogenase; D009584:Nitrogen