caa a22 4500 605507902 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1230-6 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1230-6 The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry [Elektronische Daten] [Ragnar Bjornsson, Frank Neese, Richard Schrock, Oliver Einsle, Serena DeBeer] 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. SBIC, 2014 Nitrogenase nationallicence FeMoco nationallicence Molybdenum nationallicence Model compounds nationallicence Catalysis nationallicence Bjornsson Ragnar Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany aut Neese Frank Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany aut Schrock Richard Department of Chemistry 6-331, Massachusetts Institute of Technology, 77 Massachusetts Avenue, 6-331, 02139, Cambridge, MA, USA aut Einsle Oliver Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104, Freiburg, Germany aut DeBeer Serena Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 447-460 0949-8257 20:2<447 2015 20 775 https://doi.org/10.1007/s00775-014-1230-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1230-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Bjornsson Ragnar Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany aut NATIONALLICENCE 700 1- Neese Frank Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany aut NATIONALLICENCE 700 1- Schrock Richard Department of Chemistry 6-331, Massachusetts Institute of Technology, 77 Massachusetts Avenue, 6-331, 02139, Cambridge, MA, USA aut NATIONALLICENCE 700 1- Einsle Oliver Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104, Freiburg, Germany aut NATIONALLICENCE 700 1- DeBeer Serena Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 447-460 0949-8257 20:2<447 2015 20 775