7AIZ

Vanadium nitrogenase VFe protein, high CO state

7AIZ の概要

• エントリーDOI: 10.2210/pdb7aiz/pdb
• 関連するPDBエントリー: 7ADR
• 分子名称: Nitrogenase vanadium-iron protein alpha chain, FE(8)-S(7) CLUSTER, MAGNESIUM ION, ... (12 entities in total)
• 機能のキーワード: nitrogenase, nitrogen fixation, co reduction, atomic resolution, oxidoreductase
• 由来する生物種: Azotobacter vinelandii; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 244877.82

構造登録者

Rohde, M.,Einsle, O. (登録日: 2020-09-28, 公開日: 2021-06-09, 最終更新日: 2024-01-31)

主引用文献

Rohde, M.,Laun, K.,Zebger, I.,Stripp, S.T.,Einsle, O.
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle.
Sci Adv, 7:-, 2021

PubMed Abstract: Besides its role in biological nitrogen fixation, vanadium-containing nitrogenase also reduces carbon monoxide (CO) to hydrocarbons, in analogy to the industrial Fischer-Tropsch process. The protein yields 93% of ethylene (CH), implying a C-C coupling step that mandates the simultaneous binding of two CO at the active site FeV cofactor. Spectroscopic data indicated multiple CO binding events, but structural analyses of Mo and V nitrogenase only confirmed a single site. Here, we report the structure of a two CO-bound state of V nitrogenase at 1.05 Å resolution, with one μ-bridging and one terminal CO molecule. This additional, specific ligand binding site suggests a mechanistic route for CO reduction and hydrocarbon formation, as well as a second access pathway for protons required during the reaction. Moreover, carbonyls are strong-field ligands that are chemically similar to mechanistically relevant hydrides that may be formed and used in a fully analogous fashion.

PubMed: 34049880
DOI: 10.1126/sciadv.abg4474

実験手法

X-RAY DIFFRACTION (1.05 Å)