The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry
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| 024 | 7 | 0 | |a 10.1007/s00775-014-1230-6 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1230-6 | ||
| 245 | 0 | 4 | |a The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry |h [Elektronische Daten] |c [Ragnar Bjornsson, Frank Neese, Richard Schrock, Oliver Einsle, Serena DeBeer] |
| 520 | 3 | |a 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. | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a Nitrogenase |2 nationallicence | |
| 690 | 7 | |a FeMoco |2 nationallicence | |
| 690 | 7 | |a Molybdenum |2 nationallicence | |
| 690 | 7 | |a Model compounds |2 nationallicence | |
| 690 | 7 | |a Catalysis |2 nationallicence | |
| 700 | 1 | |a Bjornsson |D Ragnar |u Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany |4 aut | |
| 700 | 1 | |a Neese |D Frank |u Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany |4 aut | |
| 700 | 1 | |a Schrock |D Richard |u Department of Chemistry 6-331, Massachusetts Institute of Technology, 77 Massachusetts Avenue, 6-331, 02139, Cambridge, MA, USA |4 aut | |
| 700 | 1 | |a Einsle |D Oliver |u Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104, Freiburg, Germany |4 aut | |
| 700 | 1 | |a DeBeer |D Serena |u Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 447-460 |x 0949-8257 |q 20:2<447 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1230-6 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1230-6 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bjornsson |D Ragnar |u Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Neese |D Frank |u Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Schrock |D Richard |u Department of Chemistry 6-331, Massachusetts Institute of Technology, 77 Massachusetts Avenue, 6-331, 02139, Cambridge, MA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Einsle |D Oliver |u Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104, Freiburg, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a DeBeer |D Serena |u Max-Planck-Institut für Chemische Energiekonversion, Stiftstr. 34-36, 45470, Mülheim and Der Ruhr, Germany |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 447-460 |x 0949-8257 |q 20:2<447 |1 2015 |2 20 |o 775 | ||