ArticleJournal of the American Chemical Society2018
Paradigm Shift for Radical S-Adenosyl-l-methionine Reactions: The Organometallic Intermediate Ω Is Central to Catalysis.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 93 citations in OpenAlex.
- The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism of controlled radical initiation in radical SAM GTP 3',8-cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The radical SAM enzyme NirJ cleaves off two propionate side chains with the release of acrylate during heme dThe FEBS journal · 2025Article
- Initiation, Propagation, and Termination in the Chemistry of Radical SAM Enzymes.Biochemistry · 2024Review
- Iron-sulfur cluster-dependent enzymes and molybdenum-dependent reductases in the anaerobic metabolism of human gut microbes.Metallomics : integrated biometal science · 2024Review
- Chemical Antiquity in Metabolism.Accounts of chemical research · 2024Article
- Electronic isomerism in a heterometallic nickel-iron-sulfur cluster models substrate binding and cyanide inhibition of carbon monoxide dehydrogenase.Chemical science · 2024Article
- Direct Detection of the α-Carbon Radical Intermediate Formed by OspD: Mechanistic Insights into RadicalJournal of the American Chemical Society · 2024Article
- ENDOR Spectroscopy Reveals the "Free" 5'-Deoxyadenosyl Radical in a Radical SAM Enzyme Active Site Actually is Chaperoned by Close Interaction with the Methionine-Bound [4Fe-4S]Journal of the American Chemical Society · 2024Article
- Pyruvate formate-lyase activating enzyme: The catalytically active 5'-deoxyadenosyl radical caught in the act of H-atom abstraction.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cluster-selectiveChemical science · 2023Article
- Computational Description of Alkylated Iron-Sulfur Organometallic Clusters.Journal of the American Chemical Society · 2023Article
- Mechanism of Radical Initiation in the Radical SAM Enzyme Superfamily.Annual review of biochemistry · 2023Review
- Development of aniScience · 2023Article
- Peptide Selenocysteine Substitutions Reveal Direct Substrate-Enzyme Interactions at Auxiliary Clusters in RadicalJournal of the American Chemical Society · 2023Article
- Evidence for Porphyrin-Mediated Electron Transfer in the Radical SAM Enzyme HutW.Biochemistry · 2023Article
- Five decades of metalloenzymology.The Enzymes · 2023Review
- Radical SAM enzymes: Nature's choice for radical reactions.FEBS letters · 2023Review
- Twenty Years of Radical SAM! The Genesis of the Superfamily.ACS bio & med chem Au · 2022Article
- Characterization by ENDOR Spectroscopy of the Iron-Alkyl Bond in a Synthetic Counterpart of Organometallic Intermediates in Radical SAM Enzymes.Journal of the American Chemical Society · 2022Article
Corrections and comments
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Authors and funding
19 authors at 5 institutions in 2 countries.
Funding
Abstract
Radical S-adenosyl-l-methionine (SAM) enzymes comprise a vast superfamily catalyzing diverse reactions essential to all life through homolytic SAM cleavage to liberate the highly reactive 5'-deoxyadenosyl radical (5'-dAdo·). Our recent observation of a catalytically competent organometallic intermediate Ω that forms during reaction of the radical SAM (RS) enzyme pyruvate formate-lyase activating-enzyme (PFL-AE) was therefore quite surprising, and led to the question of its broad relevance in the superfamily. We now show that Ω in PFL-AE forms as an intermediate under a variety of mixing order conditions, suggesting it is central to catalysis in this enzyme. We further demonstrate that Ω forms in a suite of RS enzymes chosen to span the totality of superfamily reaction types, implicating Ω as essential in catalysis across the RS superfamily. Finally, EPR and electron nuclear double resonance spectroscopy establish that Ω involves an Fe-C5' bond between 5'-dAdo· and the [4Fe-4S] cluster. An analogous organometallic bond is found in the well-known adenosylcobalamin (coenzyme B
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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.