ArticleProceedings of the National Academy of Sciences of the United States of America2015
Cysteine as a ligand platform in the biosynthesis of the FeFe hydrogenase H cluster.
Article in Proceedings of the National Academy of Sciences of the United States of America, 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.
- Characterization of a Heme-Binding Radical SAM Enzyme HemW fromACS bio & med chem Au · 2026Article
- Characterization of Complex-B ([Fe(κJournal 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
- 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
- Final Stages in the Biosynthesis of the [FeFe]-Hydrogenase Active Site.Angewandte Chemie (International ed. in English) · 2024Article
- Synthetic biology for improved hydrogen production in Chlamydomonas reinhardtii.Microbial biotechnology · 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
- Proposed Mechanism for the Biosynthesis of the [FeFe] Hydrogenase H-Cluster: Central Roles for the Radical SAM Enzymes HydG and HydE.ACS bio & med chem Au · 2022Review
- Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View.ACS bio & med chem Au · 2022Review
- Organometallic FeJournal of the American Chemical Society · 2022Article
- Quantum Chemical Study of a Radical Relay Mechanism for the HydG-Catalyzed Synthesis of a Fe(II)(CO)Biochemistry · 2021Article
- Biosynthesis of the [FeFe] hydrogenase H-clusterDalton transactions (Cambridge, England : 2003) · 2021Review
- 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
- 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
- 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
- Electron Paramagnetic Resonance Spectroscopic Identification of the Fe-S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE.Biochemistry · 2019Article
- Serine is the molecular source of the NH(CHChemical science · 2019Article
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8 authors.
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Abstract
Hydrogenases catalyze the redox interconversion of protons and H2, an important reaction for a number of metabolic processes and for solar fuel production. In FeFe hydrogenases, catalysis occurs at the H cluster, a metallocofactor comprising a [4Fe-4S]H subcluster coupled to a [2Fe]H subcluster bound by CO, CN(-), and azadithiolate ligands. The [2Fe]H subcluster is assembled by the maturases HydE, HydF, and HydG. HydG is a member of the radical S-adenosyl-L-methionine family of enzymes that transforms Fe and L-tyrosine into an [Fe(CO)2(CN)] synthon that is incorporated into the H cluster. Although it is thought that the site of synthon formation in HydG is the "dangler" Fe of a [5Fe] cluster, many mechanistic aspects of this chemistry remain unresolved including the full ligand set of the synthon, how the dangler Fe initially binds to HydG, and how the synthon is released at the end of the reaction. To address these questions, we herein show that L-cysteine (Cys) binds the auxiliary [4Fe-4S] cluster of HydG and further chelates the dangler Fe. We also demonstrate that a [4Fe-4S]aux[CN] species is generated during HydG catalysis, a process that entails the loss of Cys and the [Fe(CO)2(CN)] fragment; on this basis, we suggest that Cys likely completes the coordination sphere of the synthon. Thus, through spectroscopic analysis of HydG before and after the synthon is formed, we conclude that Cys serves as the ligand platform on which the synthon is built and plays a role in both Fe(2+) binding and synthon release.
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