ArticleNature communications2021
Molecular basis of enzymatic nitrogen-nitrogen formation by a family of zinc-binding cupin enzymes.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- General access to azoles through tailored nitrogen-nitrogen bond construction.Nature communications · 2026Article
- Hydrazinoacetic acid is a biosynthetic precursor of the bacterially produced nitramine,Applied and environmental microbiology · 2026Article
- tRNA-deacylase-directed discovery of biosynthetic pathways.Nature chemistry · 2026Article
- Role of Propionate Side Chain in Heme-Containing Metalloenzymes.ACS organic & inorganic Au · 2025Review
- Genome mining and characterization of a heme-dependent enzyme catalyzing intermolecular Nitrogen-Nitrogen bond formation in hydrazinosuccinic acid biosynthesis.Synthetic and systems biotechnology · 2025Article
- Structural insights into heme-iron dependent N-N bond formation enzyme LnzB.Communications chemistry · 2025Article
- 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
- Identification of a l-Threonine-Utilizing Hydrazine Synthetase for Thrazarine Biosynthesis in Streptomyces coerulescens MH802-fF5.Chembiochem : a European journal of chemical biology · 2025Article
- A heme-dependent enzyme forms the hydrazine in the antibiotic negamycin.Nature chemical biology · 2025Article
- Trimerization of 1,2-Diaminocyclohexane Catalyzed by a Metal-Organic Cage Tandem Catalyst with Dual Biomimetic Active Sites.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
- Revision of the Formycin A and Pyrazofurin Biosynthetic Pathways Reveals Specificity for d-Glutamic Acid and a CrypticJournal of the American Chemical Society · 2025Article
- Recent Developments and Challenges in the Enzymatic Formation of Nitrogen-Nitrogen Bonds.ACS catalysis · 2025Review
- Enzymatic synthesis of azide by a promiscuous N-nitrosylase.Nature chemistry · 2024Article
- Reconstitution of the Final Steps in the Biosynthesis of Valanimycin Reveals the Origin of Its Characteristic Azoxy Moiety.Angewandte Chemie (International ed. in English) · 2024Article
- O-methyltransferase-like enzyme catalyzed diazo installation in polyketide biosynthesis.Nature communications · 2023Article
- Effects of a Pirin-like protein on strain growth and spinosad biosynthesis in Saccharopolyspora spinosa.Applied microbiology and biotechnology · 2023Article
- Article
- Experimental and computational snapshots of C-C bond formation in a C-nucleoside synthase.Open biology · 2023Article
- Endowing homodimeric carbamoyltransferase GdmN with iterative functions through structural characterization and mechanistic studies.Nature communications · 2022Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecules with a nitrogen-nitrogen (N-N) bond in their structures exhibit various biological activities and other unique properties. A few microbial proteins are recently emerging as dedicated N-N bond forming enzymes in natural product biosynthesis. However, the details of these biochemical processes remain largely unknown. Here, through in vitro biochemical characterization and computational studies, we report the molecular basis of hydrazine bond formation by a family of di-domain enzymes. These enzymes are widespread in bacteria and sometimes naturally exist as two standalone enzymes. We reveal that the methionyl-tRNA synthase-like domain/protein catalyzes ATP-dependent condensation of two amino acids substrates to form a highly unstable ester intermediate, which is subsequently captured by the zinc-binding cupin domain/protein and undergoes redox-neutral intramolecular rearrangement to give the N-N bond containing product. These results provide important mechanistic insights into enzymatic N-N bond formation and should facilitate future development of novel N-N forming biocatalyst.
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