ArticleBiochemistry2018
X-ray and EPR Characterization of the Auxiliary Fe-S Clusters in the Radical SAM Enzyme PqqE.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- TheMolecules (Basel, Switzerland) · 2025Review
- Radical SAM Enzyme WprB Catalyzes Uniform Cross-Link Topology between Trp-C5 and Arg-Cγ on the Precursor Peptide.ACS chemical biology · 2025Article
- Hydrogen-Deuterium Exchange Mass Spectrometry Identifies Local and Long-Distance Interactions within the Multicomponent Radical SAM Enzyme, PqqE.ACS central science · 2024Article
- Structural, Biochemical, and Bioinformatic Basis for Identifying Radical SAM Cyclopropyl Synthases.ACS chemical biology · 2024Article
- Microbial synthesis of pyrroloquinoline quinone.World journal of microbiology & biotechnology · 2023Review
- The Radical SAM Heme Synthase AhbD fromBiomolecules · 2023Article
- Catalytic Site Proximity Profiling for Functional Unification of Sequence-Diverse RadicalACS bio & med chem Au · 2023Article
- How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery.ACS bio & med chem Au · 2022Review
- Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy.Applied magnetic resonance · 2022Review
- HygY Is a Twitch Radical SAM Epimerase with Latent Dehydrogenase Activity Revealed upon Mutation of a Single Cysteine Residue.Journal of the American Chemical Society · 2021Article
- 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
- 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
- Electron Paramagnetic Resonance Spectroscopic Identification of the Fe-S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE.Biochemistry · 2019Article
- Reconstitution and Substrate Specificity of the Thioether-Forming RadicalACS chemical biology · 2019Article
- Bioinformatic Mapping of Radical S-Adenosylmethionine-Dependent Ribosomally Synthesized and Post-Translationally Modified Peptides Identifies New Cα, Cβ, and Cγ-Linked Thioether-Containing Peptides.Journal of the American Chemical Society · 2019Article
- Spectroscopic and Electrochemical Characterization of the Mycofactocin Biosynthetic Protein, MftC, Provides Insight into Its Redox Flipping Mechanism.Biochemistry · 2019Article
- Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase.The Journal of biological chemistry · 2018Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The Radical SAM (RS) enzyme PqqE catalyzes the first step in the biosynthesis of the bacterial cofactor pyrroloquinoline quinone, forming a new carbon-carbon bond between two side chains within the ribosomally synthesized peptide substrate PqqA. In addition to the active site RS 4Fe-4S cluster, PqqE is predicted to have two auxiliary Fe-S clusters, like the other members of the SPASM domain family. Here we identify these sites and examine their structure using a combination of X-ray crystallography and Mössbauer and electron paramagnetic resonance (EPR) spectroscopies. X-ray crystallography allows us to identify the ligands to each of the two auxiliary clusters at the C-terminal region of the protein. The auxiliary cluster nearest the RS site (AuxI) is in the form of a 2Fe-2S cluster ligated by four cysteines, an Fe-S center not seen previously in other SPASM domain proteins; this assignment is further supported by Mössbauer and EPR spectroscopies. The second, more remote cluster (AuxII) is a 4Fe-4S center that is ligated by three cysteine residues and one aspartate residue. In addition, we examined the roles these ligands play in catalysis by the RS and AuxII clusters using site-directed mutagenesis coupled with EPR spectroscopy. Lastly, we discuss the possible functional consequences that these unique AuxI and AuxII clusters may have in catalysis for PqqE and how these may extend to additional RS enzymes catalyzing the post-translational modification of ribosomally encoded peptides.
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