title: The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry.
abstract: Biological nitrogen fixation is enabled by molybdenum-dependent nitrogenase enzymes, which effect the reduction of dinitrogen to ammonia using an Fe7MoS9C active site, referred to as the iron molybdenum cofactor or FeMoco. In this mini-review, we summarize the current understanding of the molecular and electronic structure of FeMoco. The advances in our understanding of the active site structure are placed in context with the parallel evolution of synthetic model studies. The recent discovery of Mo(III) in the FeMoco active site is highlighted with an emphasis placed on the important role that model studies have played in this finding. In addition, the reactivities of synthetic models are discussed in terms of their relevance to the enzymatic system.
authors.affiliation: Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany, ragnarbj@hi.is.
authors.forename: Ragnar
authors.initials: R
authors.lastname: Bjornsson
authors.forename: Frank
authors.initials: F
authors.lastname: Neese
authors.forename: Richard R
authors.initials: RR
authors.lastname: Schrock
authors.forename: Oliver
authors.initials: O
authors.lastname: Einsle
authors.forename: Serena
authors.initials: S
authors.lastname: DeBeer
mesh_terms: D001059:Apoproteins / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D007501:Iron / Q000737:chemistry; D008958:Models, Molecular; D008982:Molybdenum / Q000737:chemistry; D008983:Molybdoferredoxin / Q000737:chemistry* / Q000378:metabolism; D009586:Nitrogen Fixation; D011487:Protein Conformation
chemical_list: D001059:Apoproteins; D008983:Molybdoferredoxin; C065636:nitrogenase apomolybdenum-iron protein, Bacteria; D008982:Molybdenum; D007501:Iron