9R5I

Dimeric state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus in crystalline form 3

Summary for 9R5I

• Entry DOI: 10.2210/pdb9r5i/pdb
• Descriptor: F420-reducing [NiFe]-hydrogenase from Methanothermococcus thermolithotrophicus subunit alpha, NICKEL (II) ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (14 entities in total)
• Functional Keywords: [nife]-hydrogenase, redox cycle, catalysis, [4fe-4s]-cluster, f420 cofactor, fad, hydrogen activation, thermophilic methanogen, oxidoreductase
• Biological source: Methanothermococcus thermolithotrophicus DSM 2095; More
• Total number of polymer chains: 6
• Total formula weight: 214299.24

Authors

Jespersen, M.,Lemaire, O.N.,Wagner, T. (deposition date: 2025-05-08, release date: 2025-10-22, Last modification date: 2026-09-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.13 Å)