ReviewThe Journal of biological chemistry2015
Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.
Review in The Journal of biological chemistry, 2015. 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, 25 citations in OpenAlex.
- BioIron: Origin, Chemical Properties, and Biological Functions.Advances in experimental medicine and biology · 2025Review
- Amino Acids in the Root Exudates of Agave lechuguilla Torr. Favor the Recruitment and Enzymatic Activity of Nutrient-Improvement Rhizobacteria.Microbial ecology · 2023Article
- Proteomic Analysis of Methanococcus voltae Grown in the Presence of Mineral and Nonmineral Sources of Iron and Sulfur.Microbiology spectrum · 2022Article
- HydG, the "dangler" iron, and catalytic production of free CO and CNDalton transactions (Cambridge, England : 2003) · 2021Article
- 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
- Iron Carbide-Sulfide Carbonyl Clusters.Inorganic chemistry · 2019Article
- Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019Review
- Electron-Rich, Diiron Bis(monothiolato) Carbonyls: C-S Bond Homolysis in a Mixed Valence Diiron Dithiolate.Inorganic chemistry · 2018Article
- The radical SAM protein HemW is a heme chaperone.The Journal of biological chemistry · 2018Article
- Article
- Catalytic Promiscuity of the Radical S-adenosyl-L-methionine Enzyme NosL.Frontiers in chemistry · 2016Review
- Introduction to the thematic minireview series on radical S-adenosylmethionine (SAM) enzymes.The Journal of biological chemistry · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrogenase, [FeFe]-hydrogenase, and [Fe]-hydrogenase enzymes perform catalysis at metal cofactors with biologically unusual non-protein ligands. The FeMo cofactor of nitrogenase has a MoFe7S9 cluster with a central carbon, whereas the H-cluster of [FeFe]-hydrogenase contains a 2Fe subcluster coordinated by cyanide and CO ligands as well as dithiomethylamine; the [Fe]-hydrogenase cofactor has CO and guanylylpyridinol ligands at a mononuclear iron site. Intriguingly, radical S-adenosyl-L-methionine enzymes are vital for the assembly of all three of these diverse cofactors. This minireview presents and discusses the current state of knowledge of the radical S-adenosylmethionine enzymes required for synthesis of these remarkable metal cofactors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.