7JRF

CO-CO-BOUND NITROGENASE MOFE-PROTEIN FROM A. VINELANDII

7JRF の概要

• エントリーDOI: 10.2210/pdb7jrf/pdb
• 分子名称: Nitrogenase molybdenum-iron protein alpha chain, MAGNESIUM ION, Nitrogenase molybdenum-iron protein beta chain, ... (11 entities in total)
• 機能のキーワード: nitrogenase, femo-cofactor, inhibition, oxidoreductase
• 由来する生物種: Azotobacter vinelandii; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 233924.99

構造登録者

Spatzal, T.,Perez, K.A.,Buscagan, T.M.,Maggiolo, A.O.,Rees, D.C. (登録日: 2020-08-12, 公開日: 2021-03-24, 最終更新日: 2023-10-18)

主引用文献

Buscagan, T.M.,Perez, K.A.,Maggiolo, A.O.,Rees, D.C.,Spatzal, T.
Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site.
Angew.Chem.Int.Ed.Engl., 60:5704-5707, 2021

PubMed 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.

PubMed: 33320413
DOI: 10.1002/anie.202015751

実験手法

X-RAY DIFFRACTION (1.33 Å)