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  Identification of a spin-coupled Mo(III) in the nitrogenase iron–molybdenum cofactor

Bjornsson, R., Lima, F. A., Spatzal, T., Weyhermüller, T., Glatzel, P., Bill, E., et al. (2014). Identification of a spin-coupled Mo(III) in the nitrogenase iron–molybdenum cofactor. Chemical Science, 5(8), 3096-3103. doi:10.1039/C4SC00337C.

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 Creators:
Bjornsson, Ragnar1, Author              
Lima, Frederico A.1, Author              
Spatzal, Thomas2, Author
Weyhermüller, Thomas1, Author              
Glatzel, Pieter3, Author
Bill, Eckhard1, Author              
Einsle, Oliver2, Author
Neese, Frank1, Author              
DeBeer, Serena1, 4, Author              
Affiliations:
1Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
2Institute for Biochemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany, ou_persistent22              
3European Synchrotron Radiation Facility, Boĩte Postale 220, 38043 Grenoble Cedex, France, ou_persistent22              
4Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA, ou_persistent22              

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 Abstract: Nitrogenase is a complex enzyme that catalyzes the formation of ammonia utilizing a MoFe7S9C cluster. The presence of a central carbon atom was recently revealed, finally completing the atomic level description of the active site. However, important prerequisites for understanding the mechanism – the total charge, metal oxidation states and electronic structure are unknown. Herein we present high-energy resolution fluorescence detected Mo K-edge X-ray absorption spectroscopy of nitrogenase. Comparison to FeMo model complexes of known oxidation state indicates that the Mo in the FeMo cofactor of nitrogenase is best described as Mo(III), in contrast to the universally accepted Mo(IV) assignment. The oxidation state assignment is supported by theoretical calculations, which reveal the presence of an unusual spin-coupled Mo(III) site. Although so far Mo(III) was not reported to occur in biology the suggestion raises interesting parallels with the known homogenous Mo catalysts for N2 reduction, where a Mo(III) compound is the N2-binding species. It also requires a reassignment of the Fe oxidation states in the cofactor.

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Language(s): eng - English
 Dates: 2014-01-302014-04-092014-08-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C4SC00337C
 Degree: -

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Title: Chemical Science
  Abbreviation : Chem. Sci.
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: - Volume / Issue: 5 (8) Sequence Number: - Start / End Page: 3096 - 3103 Identifier: ISSN: 2041-6520
CoNE: https://pure.mpg.de/cone/journals/resource/2041-6520