Structural Enzymology of Nitrogenase Enzymes
Year: 2020
Type: review
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 N 2 . 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 N 2 and NH 3, 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.
Source: Chemical Reviews
Authors: Oliver Einsle, Douglas C. Rees
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: green
Awards: G1279010855, SPP 1927: IronSulfur for Life, Crystallographic Studies of Electron Tranfer Proteins, G6763299599, G7012460540, GRK 1976: Funktionelle Diversität von Cofaktoren in Enzymen, Nitrogenase and Nitrous Oxide Reductase:Biomolecular Engineering of Complex Redox Enzymes, Crystallographic Studies of Electron Transfer Proteins, G9000234737
OpenAlex ID: W3035190513