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          Institute: MPI für bioanorganische Chemie     Collection: MPI für bioanorganische Chemie     Display Documents

ID: 712720.0, MPI für bioanorganische Chemie / MPI für bioanorganische Chemie
The discovery of Mo(III) in FeMoco: reuniting enzyme and model chemistry
Authors:Bjornsson, Ragnar; Neese, Frank; Schrock, Richard R.; Einsle, Oliver; DeBeer, Serena
Date of Publication (YYYY-MM-DD):2015
Title of Journal:Journal of Biological Inorganic Chemistry
Journal Abbrev.:J. Biol. Inorg. Chem.
Issue / Number:2
Start Page:447
End Page:460
Review Status:Internal review
Audience:Experts Only
Abstract / Description: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.
Comment of the Author/Creator:Date: 2015, MAR 2015
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für bioanorganische Chemie
External Affiliations:[Schrock,R.R.;]Department of Chemistry 6-331, Massachusetts Institute of Technology, 77 Massachusetts Avenue, 6-331, C ambridge, MA, 02139, USA.
[Einsle,O.]Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104, Freiburg, Germany.
Identifiers:ISI:000350236100022 [ID No:1]
ISSN:0949-8257 [ID No:2]
DOI:10.1007/s00775-014-1230-6 [ID No:3]
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