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Structural Enzymology of Nitrogenase Enzymes

Einsle, Oliver and Rees, Douglas C. (2020) Structural Enzymology of Nitrogenase Enzymes. Chemical Reviews, 120 (12). pp. 4969-5004. ISSN 0009-2665. https://resolver.caltech.edu/CaltechAUTHORS:20200615-133406983

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Abstract

The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography involving two component proteins, MgATP and reductant. At center stage of this process resides the active site cofactor, a complex metallocluster organized around a trigonal prismatic arrangement of iron sites surrounding an interstitial carbon. As a consequence of the choreography, electrons and protons are delivered to the active site for transfer to the bound N₂. While the detailed mechanism for the substrate reduction remains enigmatic, recent developments highlight the role of hydrides and the privileged role for two irons of the trigonal prism in the binding of exogenous ligands. Outstanding questions concern the precise nature of the intermediates between N₂ and NH₃, and whether the cofactor undergoes significant rearrangement during turnover; resolution of these issues will require the convergence of biochemistry, structure, spectroscopy, computation, and model chemistry.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1021/acs.chemrev.0c00067DOIArticle
ORCID:
AuthorORCID
Einsle, Oliver0000-0001-8722-2893
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 2020 American Chemical Society. Received: January 26, 2020; Publication Date: June 15, 2020. This article is part of the Reactivity of Nitrogen from the Ground to the Atmosphere special issue. Research in the Einsle group was supported by Deutsche Forschungsgemeinschaft, RTG 1976 (project ID 235777276) and PP 1927 (project ID 273919336) and the European Research Council (grant no. 310656). Research in the Rees group was supported by US National Institutes of Health grant GM045162 and the Howard Hughes Medical Institute. Stimulating discussions with James B. Howard and members of the Einsle and Rees research groups are gratefully acknowledged. The authors declare no competing financial interest.
Funders:
Funding AgencyGrant Number
Deutsche Forschungsgemeinschaft (DFG)RTG 1976
Deutsche Forschungsgemeinschaft (DFG)235777276
Deutsche Forschungsgemeinschaft (DFG)PP 1927
Deutsche Forschungsgemeinschaft (DFG)273919336
NIHGM045162
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Issue or Number:12
Record Number:CaltechAUTHORS:20200615-133406983
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20200615-133406983
Official Citation:Structural Enzymology of Nitrogenase Enzymes. Oliver Einsle and Douglas C. Rees. Chemical Reviews 2020 120 (12), 4969-5004; DOI: 10.1021/acs.chemrev.0c00067
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:103924
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:15 Jun 2020 20:58
Last Modified:26 Jun 2020 15:25

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