ArticleNature chemical biology2013
Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 123 citations in OpenAlex.
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- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Regulatory networks of iron sulfur cluster biology in cancer mechanisms and therapeutic perspectives.iScience · 2026Review
- Radical Propagation via σ-Cleavage Mediates Radical SAM Catalyzed Sulfur-for-Oxygen Swapping Reaction during the Biosynthesis of Albomycin δJournal of the American Chemical Society · 2025Article
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- Alternate routes to mnmJournal of bacteriology · 2024Article
- Structure-based insights into the mechanism of [4Fe-4S]-dependent sulfur insertase LarE.Protein science : a publication of the Protein Society · 2024Article
- Discovery of a Biotin Synthase That Utilizes an Auxiliary 4Fe-5S Cluster for Sulfur Insertion.Journal of the American Chemical Society · 2024Article
- Monitoring Fe-S cluster occupancy across the E. coli proteome using chemoproteomics.Nature chemical biology · 2023Article
- Essentiality of theInternational journal of molecular sciences · 2023Article
- Biochemical and genetic studies define the functions of methylthiotransferases in methanogenic and methanotrophic archaea.Frontiers in microbiology · 2023Article
- Characterization of LipS1 and LipS2 fromACS bio & med chem Au · 2022Article
- Article
- ThnL, a B12-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- A tRNA modifying enzyme as a tunable regulatory nexus for bacterial stress responses and virulence.Nucleic acids research · 2022Article
- Investigation of bacterial diversity inBioengineered · 2021Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
14 authors at 9 institutions in 3 countries.
Funding
Abstract
How living organisms create carbon-sulfur bonds during the biosynthesis of critical sulfur-containing compounds is still poorly understood. The methylthiotransferases MiaB and RimO catalyze sulfur insertion into tRNAs and ribosomal protein S12, respectively. Both belong to a subgroup of radical-S-adenosylmethionine (radical-SAM) enzymes that bear two [4Fe-4S] clusters. One cluster binds S-adenosylmethionine and generates an Ado• radical via a well-established mechanism. However, the precise role of the second cluster is unclear. For some sulfur-inserting radical-SAM enzymes, this cluster has been proposed to act as a sacrificial source of sulfur for the reaction. In this paper, we report parallel enzymological, spectroscopic and crystallographic investigations of RimO and MiaB, which provide what is to our knowledge the first evidence that these enzymes are true catalysts and support a new sulfation mechanism involving activation of an exogenous sulfur cosubstrate at an exchangeable coordination site on the second cluster, which remains intact during the reaction.
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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.