ArticleBiochemistry2015
[FeFe]-hydrogenase maturation: insights into the role HydE plays in dithiomethylamine biosynthesis.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- 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
- Role of ammonia-lyases in the synthesis of the dithiomethylamine ligand during [FeFe]-hydrogenase maturation.The Journal of biological chemistry · 2024Article
- The H-cluster of [FeFe] Hydrogenases: Its Enzymatic Synthesis and Parallel Inorganic Semisynthesis.Accounts of chemical research · 2024Article
- Genome-Scale Mining of Acetogens of the GenusMicrobiology spectrum · 2022Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- [FeFe]-Hydrogenase: Defined Lysate-Free Maturation Reveals a Key Role for Lipoyl-H-Protein in DTMA Ligand Biosynthesis.Angewandte Chemie (International ed. in English) · 2022Article
- Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View.ACS bio & med chem Au · 2022Review
- HydG, the "dangler" iron, and catalytic production of free CO and CNDalton transactions (Cambridge, England : 2003) · 2021Article
- Crystal Structure of the [FeFe]-Hydrogenase Maturase HydE Bound to Complex-B.Journal of the American Chemical Society · 2021Article
- Article
- Active-Site Controlled, Jahn-Teller Enabled Regioselectivity in Reductive S-C Bond Cleavage ofJournal of the American Chemical Society · 2021Article
- Bioassembly of complex iron-sulfur enzymes: hydrogenases and nitrogenases.Nature reviews. Chemistry · 2020Article
- Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.Chemical science · 2020Review
- The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.The Journal of biological chemistry · 2020Article
- [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Radical SAM Enzyme HydE Generates Adenosylated Fe(I) Intermediates En Route to the [FeFe]-Hydrogenase Catalytic H-Cluster.Journal of the American Chemical Society · 2020Article
- A strategy for large-scale comparison of evolutionary- and reaction-based classifications of enzyme function.Database : the journal of biological databases and curation · 2020Article
- Serine is the molecular source of the NH(CHChemical science · 2019Article
- The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO)Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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10 authors.
Funding
Abstract
HydE and HydG are radical S-adenosyl-l-methionine enzymes required for the maturation of [FeFe]-hydrogenase (HydA) and produce the nonprotein organic ligands characteristic of its unique catalytic cluster. The catalytic cluster of HydA (the H-cluster) is a typical [4Fe-4S] cubane bridged to a 2Fe-subcluster that contains two carbon monoxides, three cyanides, and a bridging dithiomethylamine as ligands. While recent studies have shed light on the nature of diatomic ligand biosynthesis by HydG, little information exists on the function of HydE. Herein, we present biochemical, spectroscopic, bioinformatic, and molecular modeling data that together map the active site and provide significant insight into the role of HydE in H-cluster biosynthesis. Electron paramagnetic resonance and UV-visible spectroscopic studies demonstrate that reconstituted HydE binds two [4Fe-4S] clusters and copurifies with S-adenosyl-l-methionine. Incorporation of deuterium from D2O into 5'-deoxyadenosine, the cleavage product of S-adenosyl-l-methionine, coupled with molecular docking experiments suggests that the HydE substrate contains a thiol functional group. This information, along with HydE sequence similarity and genome context networks, has allowed us to redefine the presumed mechanism for HydE away from BioB-like sulfur insertion chemistry; these data collectively suggest that the source of the sulfur atoms in the dithiomethylamine bridge of the H-cluster is likely derived from HydE's thiol containing substrate.
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