ArticleAngewandte Chemie (International ed. in English)2025
Biocatalytic Olefin Difunctionalization for Synthesis of Chiral 2-Azidoamines Using Nonheme Iron Enzymes.
Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- A binuclear copper enzyme platform for enantioconvergent radical (pseudo)halogenation.bioRxiv : the preprint server for biology · 2026Article
- CURE-ating the Substrate Scope and Functional Residues of Nonheme Iron(II) α-Ketoglutarate-Dependent Hydroxylase BesE.Journal of natural products · 2026Article
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6 authors.
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Abstract
Alkene difunctionalization represents an important category of reactions in organic synthesis, with a diverse array of transformations developed over the past decades for various synthetic applications. Nevertheless, the scope and diversity of biocatalytic alkene difunctionalization have been limited, constraining its synthetic utility. In this study, we repurposed nonheme iron enzymes to generate iron nitrene intermediates for alkene difunctionalization. 4-hydroxymandelate synthase from Amycolatopsis orientalis (AoHMS) was successfully engineered for direct alkene aminoazidation to produce chiral 2-azidoamines. Directed evolution was performed on AoHMS to provide evolved variants that could utilize O-pivaloylhydroxylamine triflic acid as the nitrene precursor and produced various primary aminoazidation products with up to 44% yield, 44 total turnover number (TTN), and 98.5:1.5 enantiomeric ratio (e.r.). Mechanistic studies indicated that this new biocatalytic transformation proceeds through a stepwise radical addition and azide recombination pathway. This work expands the catalytic toolbox of metalloenzymes and opens up new opportunities for biosynthesis by introducing nonnatural olefin difunctionalization reactions into biocatalysis.
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