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  The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry

Bjornsson, R., Neese, F., Schrock, R. R., Einsle, O., & DeBeer, S. (2015). The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry. Journal of Biological Inorganic Chemistry, 20(2), 447-460. doi:10.1007/s00775-014-1230-6.

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Genre: Journal Article

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 Creators:
Bjornsson, Ragnar1, 2, Author              
Neese, Frank1, Author              
Schrock, Richard R.3, Author
Einsle, Oliver4, Author
DeBeer, Serena1, 5, Author              
Affiliations:
1Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
2Science Institute, University of Iceland, Dunhagi 3, IS-107, Reykjavik, Iceland, ou_persistent22              
3Department of Chemistry 6-331, Massachusetts Institute of Technology, 77 Massachusetts Avenue, 6-331, Cambridge, MA, 02139, USA, ou_persistent22              
4Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104, Freiburg, Germany, ou_persistent22              
5Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, 14853, USA, ou_persistent22              

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Free keywords: Nitrogenase; FeMoco; Molybdenum; Model compounds; Cataylsis
 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.

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Language(s): eng - English
 Dates: 2014-08-312014-12-312015-03-01
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s00775-014-1230-6
 Degree: -

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Title: Journal of Biological Inorganic Chemistry
  Abbreviation : J. Biol. Inorg. Chem.
Source Genre: Journal
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Publ. Info: Berlin : Springer
Pages: - Volume / Issue: 20 (2) Sequence Number: - Start / End Page: 447 - 460 Identifier: ISSN: 0949-8257
CoNE: https://pure.mpg.de/cone/journals/resource/954925573943