Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site. (27th January 2021)

• Record Type: Journal Article
• Authors: Buscagan, Trixia M.; Perez, Kathryn A.; Maggiolo, Ailiena O.; Rees, Douglas C.; Spatzal, Thomas
• Is Part Of: Angewandte Chemie. Volume 133:Number 11(2021)
• Page Start: 5768
• Page End: 5771
• Publication Date: 2021-01-27
• Subjects: carbonyl ligands -- C−C coupling -- cofactors -- nitrogenases -- X-ray diffraction; Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.202015751
• Languages: English
• ISSNs: 0044-8249

Abstract

Abstract: As an approach towards unraveling the nitrogenase mechanism, we have studied the binding of CO to the active‐site FeMo‐cofactor. CO is not only an inhibitor of nitrogenase, but it is also a substrate, undergoing reduction to hydrocarbons (Fischer–Tropsch‐type chemistry). The C−C bond forming capabilities of nitrogenase suggest that multiple CO or CO‐derived ligands bind to the active site. Herein, we report a crystal structure with two CO ligands coordinated to the FeMo‐cofactor of the molybdenum nitrogenase at 1.33 Å resolution. In addition to the previously observed bridging CO ligand between Fe2 and Fe6 of the FeMo‐cofactor, a new ligand binding mode is revealed through a second CO ligand coordinated terminally to Fe6. While the relevance of this state to nitrogenase‐catalyzed reactions remains to be established, it highlights the privileged roles for Fe2 and Fe6 in ligand binding, with multiple coordination modes available depending on the ligand and reaction conditions. Abstract : Besides reducing dinitrogen, nitrogenases reduce CO to hydrocarbons, mediating C−C bond formation between multiple CO‐derived ligands. To shed light on how multiple C‐based ligands bind to the active site, we report a 1.33 Å resolution crystal structure of two CO ligands coordinated to the FeMo‐cofactor of molybdenum nitrogenase (see picture). The second CO ligand is coordinated to Fe6 in a previously unreported ligand binding mode.