9R52
Dimeric state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus in crystalline form 2
Summary for 9R52
| Entry DOI | 10.2210/pdb9r52/pdb |
| Descriptor | F420-reducing [NiFe]-hydrogenase from Methanothermococcus thermolithotrophicus alpha subunit, F420-reducing [NiFe]-hydrogenase from Methanothermococcus thermolithotrophicus beta subunit, F420-reducing [NiFe]-hydrogenase from Methanothermococcus thermolithotrophicus gamma subunit, ... (9 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 | 3 |
| Total formula weight | 106421.42 |
| Authors | Jespersen, M.,Lemaire, O.N.,Wagner, T. (deposition date: 2025-05-08, release date: 2025-10-22, Last modification date: 2025-11-19) |
| 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 Cited by 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: 41078086DOI: 10.1002/cbic.202500692 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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