ArticleChemical science2016
The auxiliary [4Fe-4S] cluster of the Radical SAM heme synthase from
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Trapping the substrate radical of heme synthase AhbD.Frontiers in chemistry · 2024Article
- The alternative coproporphyrinogen III oxidase (CgoN) catalyzes the oxygen-independent conversion of coproporphyrinogen III into coproporphyrin III.Frontiers in microbiology · 2024Article
- The Radical SAM Heme Synthase AhbD fromBiomolecules · 2023Article
- Peptide Selenocysteine Substitutions Reveal Direct Substrate-Enzyme Interactions at Auxiliary Clusters in RadicalJournal of the American Chemical Society · 2023Article
- Point mutation of V252 in neomycin C epimerase enlarges substrate-binding pocket and improves neomycin B accumulation in Streptomyces fradiae.Bioresources and bioprocessing · 2022Article
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- Radical SAM Enzymes Involved in Tetrapyrrole Biosynthesis and Insertion.ACS bio & med chem Au · 2022Review
- RadicalJournal of the American Chemical Society · 2022Article
- 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
- Structural Properties and Catalytic Implications of the SPASM Domain Iron-Sulfur Clusters inJournal of the American Chemical Society · 2020Article
- A Radical Clock Probe Uncouples H Atom Abstraction from Thioether Cross-Link Formation by the Radical S-Adenosyl-l-methionine Enzyme SkfB.Biochemistry · 2018Article
- The radical SAM protein HemW is a heme chaperone.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heme synthase AhbD catalyzes the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme during the alternative heme biosynthesis pathway occurring in sulfate-reducing bacteria and archaea. AhbD belongs to the family of Radical SAM enzymes and contains two [4Fe-4S] clusters. Whereas one of these clusters is required for substrate radical formation, the role of the second iron-sulfur cluster is not known. In this study, the function of the auxiliary cluster during AhbD catalysis was investigated. Two single cluster variants of AhbD from
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Registered trials
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.