8BJ7

Desulfovibrio desulfuricans FeFe Hydrogenase C178A mutant in Hinact-like state

8BJ7 の概要

• エントリーDOI: 10.2210/pdb8bj7/pdb
• 関連するPDBエントリー: 1HFE 6SG2
• 分子名称: Periplasmic [Fe] hydrogenase large subunit, Periplasmic [Fe] hydrogenase small subunit, IRON/SULFUR CLUSTER, ... (5 entities in total)
• 機能のキーワード: [fefe] hydrogenase, c178a mutant, oxidoreductase
• 由来する生物種: Desulfovibrio desulfuricans; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54710.01

構造登録者

Bikbaev, K.,Span, I. (登録日: 2022-11-03, 公開日: 2023-03-22, 最終更新日: 2024-02-07)

主引用文献

Martini, M.A.,Bikbaev, K.,Pang, Y.,Lorent, C.,Wiemann, C.,Breuer, N.,Zebger, I.,DeBeer, S.,Span, I.,Bjornsson, R.,Birrell, J.A.,Rodriguez-Macia, P.
Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.
Chem Sci, 14:2826-2838, 2023

PubMed Abstract: [FeFe] hydrogenases are highly efficient metalloenyzmes for hydrogen conversion. Their active site cofactor (the H-cluster) is composed of a canonical [4Fe-4S] cluster ([4Fe-4S]) linked to a unique organometallic di-iron subcluster ([2Fe]). In [2Fe] the two Fe ions are coordinated by a bridging 2-azapropane-1,3-dithiolate (ADT) ligand, three CO and two CN ligands, leaving an open coordination site on one Fe where substrates (H and H) as well as inhibitors ( O, CO, HS) may bind. Here, we investigate two new active site states that accumulate in [FeFe] hydrogenase variants where the cysteine (Cys) in the proton transfer pathway is mutated to alanine (Ala). Our experimental data, including atomic resolution crystal structures and supported by calculations, suggest that in these two states a third CN ligand is bound to the apical position of [2Fe]. These states can be generated both by "cannibalization" of CN from damaged [2Fe] subclusters as well as by addition of exogenous CN. This is the first detailed spectroscopic and computational characterisation of the interaction of exogenous CN with [FeFe] hydrogenases. Similar CN-bound states can also be generated in wild-type hydrogenases, but do not form as readily as with the Cys to Ala variants. These results highlight how the interaction between the first amino acid in the proton transfer pathway and the active site tunes ligand binding to the open coordination site and affects the electronic structure of the H-cluster.

PubMed: 36937599
DOI: 10.1039/d2sc06098a

実験手法

X-RAY DIFFRACTION (1.04 Å)