{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["12"],"submitter":["Heidinger L"],"pubmed_abstract":["The heme synthase AhbD catalyzes the last step of the siroheme-dependent heme biosynthesis pathway, which is operative in archaea and sulfate-reducing bacteria. The AhbD-catalyzed reaction consists of the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme <i>b</i>. AhbD is a Radical SAM enzyme employing radical chemistry to achieve the decarboxylation reaction. Previously, it was proposed that the central iron ion of the substrate iron-coproporphyrin III participates in the reaction by enabling electron transfer from the initially formed substrate radical to an iron-sulfur cluster in AhbD. In this study, we investigated the substrate radical that is formed during AhbD catalysis. While the iron-coproporphyrinyl radica"],"journal":["Frontiers in chemistry"],"pagination":["1430796"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11306076"],"repository":["biostudies-literature"],"pubmed_title":["Trapping the substrate radical of heme synthase AhbD."],"pmcid":["PMC11306076"],"pubmed_authors":["Layer G","Heidinger L","Fix I","Friedrich T"],"additional_accession":[]},"is_claimable":false,"name":"Trapping the substrate radical of heme synthase AhbD.","description":"The heme synthase AhbD catalyzes the last step of the siroheme-dependent heme biosynthesis pathway, which is operative in archaea and sulfate-reducing bacteria. The AhbD-catalyzed reaction consists of the oxidative decarboxylation of two propionate side chains of iron-coproporphyrin III to the corresponding vinyl groups of heme <i>b</i>. AhbD is a Radical SAM enzyme employing radical chemistry to achieve the decarboxylation reaction. Previously, it was proposed that the central iron ion of the substrate iron-coproporphyrin III participates in the reaction by enabling electron transfer from the initially formed substrate radical to an iron-sulfur cluster in AhbD. In this study, we investigated the substrate radical that is formed during AhbD catalysis. While the iron-coproporphyrinyl radica","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2025-06-01T00:59:15.917Z","creation":"2025-06-01T00:59:15.917Z"},"accession":"S-EPMC11306076","cross_references":{"pubmed":["39119521"],"doi":["10.3389/fchem.2024.1430796"]}}