ArticleNature chemistry2024
Enzymatic synthesis of azide by a promiscuous N-nitrosylase.
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 9 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Hydrazinoacetic acid is a biosynthetic precursor of the bacterially produced nitramine,Applied and environmental microbiology · 2026Article
- Green and Sustainable Chemistry Approaches on Azide-Based Click Reactions in Polymer Science.Macromolecular rapid communications · 2025Review
- Conversion of a Heme-Dependent Dehydratase to a Piperazate Synthase Reveals the Role of the Heme Propionate Group in N-N Bond-Formation.Journal of the American Chemical Society · 2025Article
- The Role of the Unusual 2-Tyr-1-carboxylate Non-heme Iron Motif in the Mechanism of N,N-Dimethylformamidase.ACS catalysis · 2025Article
- Structural Basis for the Catalytic Mechanism of ATP-Dependent Diazotase CmaA6.Angewandte Chemie (International ed. in English) · 2025Article
- Discovery, Herbicidal Activity and Biosynthesis of a Novel Natural Tetramic Acid from Alternaria Species.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Exquisite Complex Reaction Cascade in the Natural 1,2,4-Triazine Assembly.Journal of the American Chemical Society · 2025Article
- Recent Developments and Challenges in the Enzymatic Formation of Nitrogen-Nitrogen Bonds.ACS catalysis · 2025Review
- Characterization of the Flavin-Dependent Monooxygenase Involved in the Biosynthesis of the Nocardiosis-Associated Polyketide†.Biochemistry · 2024Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Azides are energy-rich compounds with diverse representation in a broad range of scientific disciplines, including material science, synthetic chemistry, pharmaceutical science and chemical biology. Despite ubiquitous usage of the azido group, the underlying biosynthetic pathways for its formation remain largely unknown. Here we report the characterization of an enzymatic route for de novo azide construction. We demonstrate that Tri17, a promiscuous ATP- and nitrite-dependent enzyme, catalyses organic azide synthesis through sequential N-nitrosation and dehydration of aryl hydrazines. Through biochemical, structural and computational analyses, we further propose a plausible molecular mechanism for azide synthesis that sets the stage for future biocatalytic applications and biosynthetic pathway engineering.
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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.