Subunit fusion unlocks rapid in vitro maturation for slowly activating heterodimeric [FeFe]-hydrogenases

2026/01/01 by Jan Jaenecke, Konstantin Bikbaev, Miriam Malagnini +8 · 1 voice
Biochemistry, Genetics and Molecular Biology · Chemistry · Energy · #Enzyme Catalysis and Immobilization #Metal-Catalyzed Oxygenation Mechanisms #Metalloenzymes and iron-sulfur proteins

paper · pdf · doi:10.1039/d5sc07299a

openalex publication_date 2026/01/01 · openalex created_date 2026/02/04 · openalex updated_date 2026/07/30

Abstract

Subunit fusion unlocks fast maturation for slowly maturating [FeFe]-hydrogenase Dd HydAB. Linking small and large subunit stabilizes active site closure after 2Fe H uptake, accelerating H-cluster formation and activity development by 40-fold.

Citations

• UCSF ChimeraX: Tools for structure building and analysis
• Oxygen sensitivity of [FeFe]-hydrogenase: a comparative study of active site mimics inside vs. outside the enzyme
• Highly accurate protein structure prediction with AlphaFold
• Phasercrystallographic software

Discussions

• Check out this cool new paper by Martin Winkler et al. who investigate the slow maturation of [FeFe]-hydrogenase DdH. Turns out that exchanging certain peptide motives allows for significant faster H- [bsky, 6 points, 0 comments]

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