9E15

Alpha-Delta heterodimeric form of soluble hydrogenase I from Pyrococcus furiosus. Data processed and model refined in P1

9E15 の概要

• エントリーDOI: 10.2210/pdb9e15/pdb
• 分子名称: Sulfhydrogenase 1 subunit delta, Sulfhydrogenase 1 subunit alpha, IRON/SULFUR CLUSTER, ... (8 entities in total)
• 機能のキーワード: ni-fe hydrogenase, lyase
• 由来する生物種: Pyrococcus furiosus; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 635523.54

構造登録者

Lanzilotta, W.N.,McTernan, P.M.,Adams, M.W.W. (登録日: 2024-10-21, 公開日: 2025-07-16, 最終更新日: 2025-09-17)

主引用文献

Xiao, X.,Schut, G.J.,Feng, X.,McTernan, P.M.,Haja, D.K.,Lanzilotta, W.N.,Adams, M.W.W.,Li, H.
Structural insights into the biotechnologically relevant reversible NADPH-oxidizing NiFe-hydrogenase from P.furiosus.
Structure, 33:1470-1483.e3, 2025

PubMed Abstract: The cytoplasmic hydrogenase I (SHI) from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the group III hydrogenase family. SHI oxidizes NADPH rather than NADH to reduce protons and evolve hydrogen gas, and because of this property, coupled with its high thermal stability, the enzyme holds great potential for economical hydrogen production. Despite decades of efforts, the SHI structure has remained unknown. Here, we report the cryoelectron microscopic (cryo-EM) structures of the heterotetrameric SHI holoenzyme (αδβγ). SHI is a symmetric dimer of two individually functional heterotetramers. SHI-αδ resembles the standard [NiFe] hydrogenase, and SHI-βγ function as the NADPH oxidoreductase. SHI-β contains three [4Fe-4S] clusters that relay electrons from NADPH in SHI-γ to the catalytic [NiFe] cluster in SHI-αδ for H production. These structures will guide the adaptation of this unique enzyme for biotechnological applications.

PubMed: 40570843
DOI: 10.1016/j.str.2025.05.017

実験手法

X-RAY DIFFRACTION (2.6 Å)