ArticleAccounts of chemical research2024
The H-cluster of [FeFe] Hydrogenases: Its Enzymatic Synthesis and Parallel Inorganic Semisynthesis.
Article in Accounts of chemical research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Synthesis of diiron subcluster [FeNature protocols · 2026Review
- A Non-Covalent [4Fe-4S]/[2Fe] Interface in HydF Guides [FeFe]-Hydrogenase Maturation.Angewandte Chemie (International ed. in English) · 2026Article
- Biosynthesis of the Selenium-Substituted [FeFe]-Hydrogenases.Journal of the American Chemical Society · 2026Article
- Subunit fusion unlocks rapidChemical science · 2026Article
- The [4Fe-4S] Cluster of HydF Is Essential for [FeFe]-Hydrogenase Maturation.Journal of the American Chemical Society · 2025Article
- [FeInorganic chemistry · 2025Article
- In vitro maturation of fully active [FeFe]-hydrogenase in a defined system including the iron carrier NfuA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
- Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Characterization of Complex-B ([Fe(κJournal of the American Chemical Society · 2025Article
- A [FeFe] Hydrogenase-Rubrerythrin Chimeric Enzyme Functions to Couple HJournal of the American Chemical Society · 2025Article
- HydE Catalytic Mechanism Is Powered by a Radical Relay with Redox-Active Fe(I)-Containing Intermediates.Journal of the American Chemical Society · 2025Article
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3 authors.
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Abstract
Nature's prototypical hydrogen-forming catalysts─hydrogenases─have attracted much attention because they catalyze hydrogen evolution at near zero overpotential and ambient conditions. Beyond any possible applications in the energy sphere, the hydrogenases feature complicated active sites, which implies novel biosynthetic pathways. In terms of the variety of cofactors, the [FeFe]-hydrogenase is among the most complex. For more than a decade, we have worked on the biosynthesis of the active site of [FeFe] hydrogenases. This site, the H-cluster, is a six-iron ensemble consisting of a [4Fe-4S]
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