8AIO

CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI)

8AIO の概要

• エントリーDOI: 10.2210/pdb8aio/pdb
• 関連するPDBエントリー: 4XDC
• 分子名称: Iron hydrogenase 1, Binuclear [FeFe], di(thiomethyl)amine, carbon monoxide, cyanide cluster (-CO form), IRON/SULFUR CLUSTER, ... (8 entities in total)
• 機能のキーワード: [fefe]-hydrogenase, co-bound, oxidoreductase
• 由来する生物種: Clostridium pasteurianum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 134505.82

構造登録者

Duan, J.,Hofmann, E.,Happe, T. (登録日: 2022-07-26, 公開日: 2022-12-14, 最終更新日: 2024-02-07)

主引用文献

Duan, J.,Hemschemeier, A.,Burr, D.J.,Stripp, S.T.,Hofmann, E.,Happe, T.
Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.
Angew.Chem.Int.Ed.Engl., 62:e202216903-e202216903, 2023

PubMed Abstract: Hydrogenases are H converting enzymes that harbor catalytic cofactors in which iron (Fe) ions are coordinated by biologically unusual carbon monoxide (CO) and cyanide (CN ) ligands. Extrinsic CO and CN , however, inhibit hydrogenases. The mechanism by which CN binds to [FeFe]-hydrogenases is not known. Here, we obtained crystal structures of the CN -treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum. The high resolution of 1.39 Å allowed us to distinguish intrinsic CN and CO ligands and to show that extrinsic CN binds to the open coordination site of the cofactor where CO is known to bind. In contrast to other inhibitors, CN treated crystals show conformational changes of conserved residues within the proton transfer pathway which could allow a direct proton transfer between E279 and S319. This configuration has been proposed to be vital for efficient proton transfer, but has never been observed structurally.

PubMed: 36464641
DOI: 10.1002/anie.202216903

実験手法

X-RAY DIFFRACTION (1.52 Å)