Structural and Spectroscopic Insights into Catalytic Intermediates of a [NiFe]‐hydrogenase from Group 3
Hydrogenases catalyze reversible H<sub>2</sub> 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.
Authors
- Marion Jespersen (ORCID: https://orcid.org/0000-0002-8859-3335)
- Olivier N. Lemaire (ORCID: https://orcid.org/0000-0002-4389-5786)
- Ingo Zebger (ORCID: https://orcid.org/0000-0002-6354-3585)
- Tristan Wagner (ORCID: https://orcid.org/0000-0002-3382-8969)
- Christian Lorent (ORCID: https://orcid.org/0000-0001-9057-4523)
Institutions
- Centre National de la Recherche Scientifique (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- CEA Grenoble (FR)
- Max Planck Institute for Marine Microbiology (DE)
- Institut de Biologie Structurale (FR)
- Technische Universität Berlin (DE)
- Université Grenoble Alpes (FR)
Publication Details
- Journal
- ChemBioChem
- Published
- 2025-10-13
- DOI
- https://doi.org/10.1002/cbic.202500692
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00