ArticleNature chemistry2024
A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile.
Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed.
- Discovery and Biosynthesis of Nitrilobacillins by Post-Translational Introduction of C-Terminal Nitrile Groups.Journal of the American Chemical Society · 2026Article
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Discovery and Biosynthesis of Nitrilobacillins by Post-translational Introduction of C-Terminal Nitrile Groups.bioRxiv : the preprint server for biology · 2026Article
- Discovery of a Structurally Distinct Acetylenase in the Biosynthesis of Mangotoxin.Journal of the American Chemical Society · 2026Article
- Crystal structure of RohS, a heme-oxygenase-like N-oxygenase from azomycin biosynthesis.The Journal of biological chemistry · 2026Article
- Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026Review
- Microbial unusual gene clusters without prominent core enzymes: natural products, biosynthesis and genome mining.The Journal of antibiotics · 2026Review
- Azetidine amino acid biosynthesis by non-haem iron-dependent enzymes.Nature chemistry · 2026Article
- A two-metalloenzyme cascade constructs the azetidine-containing pharmacophore.Nature chemistry · 2026Article
- A ferritin-like diiron oxygenase BioE initiates bacterial biotin synthesis, a promising antivirulence target.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Discovery and Mechanism of a Diiron Enzyme in Ethylidene Azetidine Formation.Journal of the American Chemical Society · 2025Article
- Structural basis of a 2-oxoglutarate-dependent heme-oxygenase-like enzyme HamA in fragin biosynthesis.RSC advances · 2025Article
- The Heme Oxygenase-Like Diiron Enzyme HrmI Reveals Altered Regulatory Mechanisms for Dioxygen Activation and Substrate N-Oxygenation.Journal of the American Chemical Society · 2025Article
- Metagenomic Identification of Brominated Indole Biosynthetic Machinery from Cyanobacteria.Journal of natural products · 2025Article
- Mining for Halogenated Metabolites ofJournal of natural products · 2025Article
- Heme Oxygenase-Like Metalloenzymes.Annual review of biochemistry · 2025Review
- Expanding Perchlorate Use for C-H Oxidative Transformations: A Tandem Photo- and Iron-Catalytic Strategy.Organometallics · 2025Article
- Biochemical characterization of the self-sacrificing p-aminobenzoate synthase from Nitrosomonas europaea reveals key residues involved in selecting a Fe/Fe or Mn/Fe cofactor.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Single-Enzyme Conversion of Tryptophan to Skatole and Cyanide Expands the Mechanistic Competence of Diiron Oxidases.Journal of the American Chemical Society · 2025Article
- Assembly of a Heterobimetallic Fe/Mn Cofactor in theBiochemistry · 2024Article
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Abstract
Nitriles are uncommon in nature and are typically constructed from oximes through the oxidative decarboxylation of amino acid substrates or from the derivatization of carboxylic acids. Here we report a third nitrile biosynthesis strategy featuring the cyanobacterial nitrile synthase AetD. During the biosynthesis of the eagle-killing neurotoxin, aetokthonotoxin, AetD transforms the 2-aminopropionate portion of 5,7-dibromo-L-tryptophan to a nitrile. Employing a combination of structural, biochemical and biophysical techniques, we characterized AetD as a non-haem diiron enzyme that belongs to the emerging haem-oxygenase-like dimetal oxidase superfamily. High-resolution crystal structures of AetD together with the identification of catalytically relevant products provide mechanistic insights into how AetD affords this unique transformation, which we propose proceeds via an aziridine intermediate. Our work presents a unique template for nitrile biogenesis and portrays a substrate binding and metallocofactor assembly mechanism that may be shared among other haem-oxygenase-like dimetal oxidase enzymes.
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