9R51

Dimeric state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus in crystalline form 1

9R51 の概要

• エントリーDOI: 10.2210/pdb9r51/pdb
• 分子名称: F420-reducing [NiFe]-hydrogenase from Methanothermococcus thermolithotrophicus subunit alpha, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (13 entities in total)
• 機能のキーワード: [nife]-hydrogenase, redox cycle, catalysis, [4fe-4s]-cluster, f420 cofactor, fad, hydrogen activation, thermophilic methanogen, oxidoreductase
• 由来する生物種: Methanothermococcus thermolithotrophicus DSM 2095; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 427533.52

構造登録者

Jespersen, M.,Lemaire, O.N.,Wagner, T. (登録日: 2025-05-08, 公開日: 2025-10-22, 最終更新日: 2025-11-19)

主引用文献

Jespersen, M.,Lorent, C.,Lemaire, O.N.,Zebger, I.,Wagner, T.
Structural and Spectroscopic Insights into Catalytic Intermediates of a [NiFe]-hydrogenase from Group 3.
Chembiochem, 26:e202500692-e202500692, 2025

PubMed Abstract: Hydrogenases catalyze reversible H production and are potential models for renewable energy catalysts. Here, the full redox landscape of a group 3 [NiFe]-hydrogenase from methanothermococcus thermolithotrophicus is elucidated, resembling group 1 enzymes. Structural and spectroscopic analyses reveal a catalytic-ready state with nickel seesaw coordination, enabling intermediate trapping and advancing mechanistic understanding of oxygen-sensitive [NiFe] enzymes.

PubMed: 41078086
DOI: 10.1002/cbic.202500692

実験手法

X-RAY DIFFRACTION (2.3 Å)