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 Fe 7 MoS 9 C 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 evo- lution 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
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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Journal of biological inorganic chemistry : JBIC . 20, 2 (2015), 447-460, DOI 10.1007/s00775-014-1230-6, issn: 1432-1327
- Schlagwort
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Nitrogenase
Molybdän
Modellverbindung
Katalyse
Physikalische Chemie
- Ereignis
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Veröffentlichung
- (wo)
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Freiburg
- (wer)
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Universität
- (wann)
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2018
- Urheber
- Beteiligte Personen und Organisationen
- DOI
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10.1007/s00775-014-1230-6
- URN
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urn:nbn:de:bsz:25-freidok-150613
- Rechteinformation
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Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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25.03.2025, 13:53 MEZ
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Beteiligte
- Bjornsson, Ragnar
- Neese, Frank
- Schrock, Richard R.
- Einsle, Oliver
- DeBeer, Serena
- Albert-Ludwigs-Universität Freiburg. Institut für Biochemie
- Universität
Entstanden
- 2018
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