ArticleProceedings of the National Academy of Sciences of the United States of America2022
A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 39 citations in OpenAlex.
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron Oxidative Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026Article
- Discovery and Biosynthesis of Nitrilobacillins by Post-Translational Introduction of C-Terminal Nitrile Groups.Journal of the American Chemical Society · 2026Article
- Discovery and Biosynthesis of Nitrilobacillins by Post-translational Introduction of C-Terminal Nitrile Groups.bioRxiv : the preprint server for biology · 2026Article
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron-Dependent Oxidative Enzyme during RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Biosynthesis of Peptidic Thiooxazole Metallophores Installed by Multinuclear Nonheme Iron Enzymes.ACS chemical biology · 2026Article
- Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Biosynthesis of peptidic thiooxazole metallophores installed by multinuclear nonheme iron enzymes.bioRxiv : the preprint server for biology · 2025Article
- Co-opting the bacterial lipoprotein pathway in the biosynthesis of a lipidated macrocyclic peptide.bioRxiv : the preprint server for biology · 2025Article
- Phylogenomic Identification of a Highly Conserved Copper-Binding RiPP Biosynthetic Gene Cluster in MarineACS chemical biology · 2025Article
- Discovery of acylsulfenic acid-featuring natural product sulfenicin and characterization of its biosynthesis.Nature chemistry · 2025Article
- Copper-chelating natural products.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Methanobactins: Structures, Biosynthesis, and Microbial Diversity.Annual review of microbiology · 2024Review
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- A multi-iron enzyme installs copper-binding oxazolone/thioamide pairs on a nontypeableProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.Current opinion in chemical biology · 2024Review
- Initial Steps in Methanobactin Biosynthesis: Substrate Binding by the Mixed-Valent Diiron Enzyme MbnBC.Biochemistry · 2024Article
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
SignificanceMethanobactins (Mbns), copper-binding peptidic compounds produced by some bacteria, are candidate therapeutics for human diseases of copper overload. The paired oxazolone-thioamide bidentate ligands of methanobactins are generated from cysteine residues in a precursor peptide, MbnA, by the MbnBC enzyme complex. MbnBC activity depends on the presence of iron and oxygen, but the catalytically active form has not been identified. Here, we provide evidence that a dinuclear Fe(II)Fe(III) center in MbnB, which is the only representative of a >13,000-member protein family to be characterized, is responsible for this reaction. These findings expand the known roles of diiron enzymes in biology and set the stage for mechanistic understanding, and ultimately engineering, of the MbnBC biosynthetic complex.
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