8PBB

CHAPSO treated partial catalytic component (comprising only AnfD & AnfK, lacking AnfG and FeFeco) of iron nitrogenase from Rhodobacter capsulatus

8PBB の概要

• エントリーDOI: 10.2210/pdb8pbb/pdb
• 関連するPDBエントリー: 8OIE
• EMDBエントリー: 17583
• 分子名称: Nitrogenase protein alpha chain, Nitrogenase iron-iron protein, beta subunit, FE(8)-S(7) CLUSTER (3 entities in total)
• 機能のキーワード: nitrogen fixation, fe nitrogenase, oxidoreductase
• 由来する生物種: Rhodobacter capsulatus SB 1003; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 223337.46

構造登録者

Schmidt, F.V.,Schulz, L.,Zarzycki, J.,Prinz, S.,Erb, T.J.,Rebelein, J.G. (登録日: 2023-06-09, 公開日: 2023-10-04, 最終更新日: 2024-01-31)

主引用文献

Schmidt, F.V.,Schulz, L.,Zarzycki, J.,Prinz, S.,Oehlmann, N.N.,Erb, T.J.,Rebelein, J.G.
Structural insights into the iron nitrogenase complex.
Nat.Struct.Mol.Biol., 31:150-158, 2024

PubMed Abstract: Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the three nitrogenase isozymes, the iron nitrogenase has the highest wild-type activity for the reduction of CO, but the molecular architecture facilitating these activities has remained unknown. Here, we report a 2.35-Å cryogenic electron microscopy structure of the ADP·AlF-stabilized iron nitrogenase complex from Rhodobacter capsulatus, revealing an [FeSC-(R)-homocitrate] cluster in the active site. The enzyme complex suggests that the iron nitrogenase G subunit is involved in cluster stabilization and substrate channeling and confers specificity between nitrogenase reductase and catalytic component proteins. Moreover, the structure highlights a different interface between the two catalytic halves of the iron and the molybdenum nitrogenase, potentially influencing the intrasubunit 'communication' and thus the nitrogenase mechanism.

PubMed: 38062208
DOI: 10.1038/s41594-023-01124-2

実験手法

ELECTRON MICROSCOPY (2.49 Å)