ArticleBiochemistry2019
Electron Paramagnetic Resonance Spectroscopic Identification of the Fe-S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Characterization of a Heme-Binding Radical SAM Enzyme HemW fromACS bio & med chem Au · 2026Article
- Photoinduced Electron Transfer Informs on Pathway Coupling in Flavin-Based Electron Bifurcation.ACS bio & med chem Au · 2026Article
- EPR Characterization of the BlsE Substrate Radical Offers Insight into the Determinants of Reaction Outcome that Distinguish Radical SAM Dioldehydratases from Dehydrogenases.Journal of the American Chemical Society · 2025Article
- Biosynthesis of GMGT lipids by a radical SAM enzyme associated with anaerobic archaea and oxygen-deficient environments.Nature communications · 2024Article
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- Hydrogen-Deuterium Exchange Mass Spectrometry Identifies Local and Long-Distance Interactions within the Multicomponent Radical SAM Enzyme, PqqE.ACS central science · 2024Article
- Peptide Selenocysteine Substitutions Reveal Direct Substrate-Enzyme Interactions at Auxiliary Clusters in RadicalJournal of the American Chemical Society · 2023Article
- Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy.Applied magnetic resonance · 2022Review
- Trapping a cross-linked lysine-tryptophan radical in the catalytic cycle of the radical SAM enzyme SuiB.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Characterization of Paramagnetic Iron-Sulfur Clusters Using Electron Paramagnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Radical SAM Enzymes and Ribosomally-Synthesized and Post-translationally Modified Peptides: A Growing Importance in the Microbiomes.Frontiers in chemistry · 2021Review
- Biosynthesis of the sactipeptide Ruminococcin C by the human microbiome: Mechanistic insights into thioether bond formation by radical SAM enzymes.The Journal of biological chemistry · 2020Article
- Biogenesis of the peptide-derived redox cofactor pyrroloquinoline quinone.Current opinion in chemical biology · 2020Review
- Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters inJournal of the American Chemical Society · 2020Article
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4 authors.
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Abstract
Pyrroloquinoline quinone (PQQ) is an important redox active quinocofactor produced by a wide variety of bacteria. A key step in PQQ biosynthesis is a carbon-carbon cross-link reaction between glutamate and tyrosine side chains within the ribosomally synthesized peptide substrate PqqA. This reaction is catalyzed by the radical SAM enzyme PqqE. Previous X-ray crystallographic and spectroscopic studies suggested that PqqE, like the other members of the SPASM domain family, contains two auxiliary Fe-S clusters (AuxI and AuxII) in addition to the radical SAM [4Fe-4S] cluster. However, a clear assignment of the electron paramagnetic resonance (EPR) signal of each Fe-S cluster was hindered by the isolation of a His
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