ArticleNature communications2025
Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Beyond Single Enzymes: System-Level Fungal Transformation of Halogenated Nitrophenols.Journal of fungi (Basel, Switzerland) · 2026Article
- Total Synthesis and Antimalarial Studies of Caelestines A-C.ChemMedChem · 2026Article
- Biocatalytic Synthesis of Isoxazolines Enabled by Cryptic Nitrile Oxide Formation by a Vanadium-Dependent Chloroperoxidase.Angewandte Chemie (International ed. in English) · 2026Article
- Chemoenzymatic Triazolopyridine Synthesis Enabled by Cryptic Diazo Formation by Vanadium-Dependent Haloperoxidases.Organic letters · 2026Article
- Elevating Haloperoxidase Expression in Escherichia coli through Fusion with a Formate Oxidase.Chembiochem : a European journal of chemical biology · 2026Article
- Chlorination of Amines by a Vanadium-Dependent Chloroperoxidase.ACS catalysis · 2026Article
- Oxidative Rearrangement of Indoles Enabled by Promiscuous Cryptic Halogenation with Vanadium-Dependent Haloperoxidases.ACS catalysis · 2026Article
- Chemoenzymatic Diazo Synthesis Enabled by Enzymatic Halide Recycling with Vanadium-Dependent Haloperoxidases.Journal of the American Chemical Society · 2026Article
- Understanding the role of vanadium: insights into bacterial responses and adaptations.Frontiers in microbiology · 2026Review
- Separation of halide oxidation and substrate halogenation chemistries rationalizes site-selective vanadium dependent haloperoxidase catalysis.bioRxiv : the preprint server for biology · 2025Article
- Regioselective C─H Functionalization by the Combination of Enzymatic and Chemocatalytic Reactions in Water.Angewandte Chemie (International ed. in English) · 2025Article
- Biocatalytic Thioketal Cleavage Enabled by Enzymatic Bromide Recycling by Vanadium-Dependent Haloperoxidases.Organic letters · 2025Article
- Chemoenzymatic C,C-Bond Forming Cascades by Cryptic Vanadium Haloperoxidase Catalyzed Bromination.Organic letters · 2025Article
- Peptide halogenation biochemistry: interfacing pharmaceutical deliverables with chemical innovation.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2025Review
- Vanadium-dependent haloperoxidases from diverse microbes halogenate exogenous alkyl quinolone quorum sensing signals.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Vanadium-dependent haloperoxidases (VHPOs) are biotechnologically valuable and operationally versatile biocatalysts. VHPOs share remarkable active-site structural similarities yet display variable reactivity and selectivity. The factors dictating substrate specificity and, thus, a general understanding of VHPO reaction control still need to be discovered. This work's strategic single-point mutation in the cyanobacterial bromoperoxidase AmVHPO facilitates a selectivity switch to allow aryl chlorination. This mutation induces loop formation that interacts with the neighboring protein monomer, creating a tunnel to the active sites. Structural analysis of the substrate-R425S-mutant complex reveals a substrate-binding site at the interface of two adjacent units. There, residues Glu139 and Phe401 interact with arenes, extending the substrate residence time close to the vanadate cofactor and stabilizing intermediates. Our findings validate the long-debated existence of direct substrate binding and provide a detailed VHPO mechanistic understanding. This work will pave the way for a broader application of VHPOs in diverse chemical processes.
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