ArticleBiochemistry2016
A Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- The [4Fe-4S] Cluster of HydF Is Essential for [FeFe]-Hydrogenase Maturation.Journal of the American Chemical Society · 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
- 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
- HydG, the "dangler" iron, and catalytic production of free CO and CNDalton transactions (Cambridge, England : 2003) · 2021Article
- Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.Chemical science · 2020Review
- H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Radical S-adenosylmethionine maquette chemistry: CxJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Monitoring H-cluster assembly using a semi-synthetic HydF protein.Dalton transactions (Cambridge, England : 2003) · 2019Article
- Overview of the Maturation Machinery of the H-Cluster of [FeFe]-Hydrogenases with a Focus on HydF.International journal of molecular sciences · 2018Review
- Electron-Rich, Diiron Bis(monothiolato) Carbonyls: C-S Bond Homolysis in a Mixed Valence Diiron Dithiolate.Inorganic chemistry · 2018Article
- Iron-Sulfur Cluster States of the Hydrogenase Maturase HydF.Biochemistry · 2017Article
- Structural and functional characterization of the hydrogenase-maturation HydF protein.Nature chemical biology · 2017Article
- Article
- Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch.Scientific reports · 2017Article
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5 authors.
Funding
Abstract
[FeFe]-hydrogenases are nature's most prolific hydrogen catalysts, excelling at facilely interconverting H2 and protons. The catalytic core common to all [FeFe]-hydrogenases is a complex metallocofactor, referred to as the H-cluster, which is composed of a standard [4Fe-4S] cluster linked through a bridging thiolate to a 2Fe subcluster harboring dithiomethylamine, carbon monoxide, and cyanide ligands. This 2Fe subcluster is synthesized and inserted into [FeFe]-hydrogenase by three maturase enzymes denoted HydE, HydF, and HydG. HydE and HydG are radical S-adenosylmethionine enzymes and synthesize the nonprotein ligands of the H-cluster. HydF is a GTPase that functions as a scaffold or carrier for 2Fe subcluster production. Herein, we utilize UV-visible, circular dichroism, and electron paramagnetic resonance spectroscopic studies to establish the existence of redox active [4Fe-4S] and [2Fe-2S] clusters bound to HydF. We have used spectroelectrochemical titrations to assign iron-sulfur cluster midpoint potentials, have shown that HydF purifies with a reduced [2Fe-2S] cluster in the absence of exogenous reducing agents, and have tracked iron-sulfur cluster spectroscopic changes with quaternary structural perturbations. Our results provide an important foundation for understanding the maturation process by defining the iron-sulfur cluster content of HydF prior to its interaction with HydE and HydG. We speculate that the [2Fe-2S] cluster of HydF either acts as a placeholder for HydG-derived Fe(CO)2CN species or serves as a scaffold for 2Fe subcluster assembly.
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