Structural highlights
Publication Abstract from PubMed
Hydrogenases catalyze reversible H(2) 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.
Structural and Spectroscopic Insights into Catalytic Intermediates of a [NiFe]-hydrogenase from Group 3.,Jespersen M, Lorent C, Lemaire ON, Zebger I, Wagner T Chembiochem. 2025 Oct 13:e202500692. doi: 10.1002/cbic.202500692. PMID:41078086[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jespersen M, Lorent C, Lemaire ON, Zebger I, Wagner T. Structural and Spectroscopic Insights into Catalytic Intermediates of a [NiFe]-hydrogenase from Group 3. Chembiochem. 2025 Oct 13:e202500692. PMID:41078086 doi:10.1002/cbic.202500692
