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|
|Review Status:||Internal review|
|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|
|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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