{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Baumgartner JT"],"funding":["NIGMS NIH HHS"],"pubmed_abstract":["Vanadium-dependent haloperoxidases (VHPOs) catalyze the halogenation of organic molecules under mild aqueous conditions. Selective bacterial VHPOs exhibit exquisite regio- and enantiocontrol, however the precise mechanisms dictating selectivity have remained elusive. We have solved the single-particle cryo-electron microscopy (cryo-EM) structure of a selective bromoperoxidase from <i>Enhygromyxa salina</i> (esVHPO). Mutagenesis demonstrates that halide oxidation and substrate halogenation occur in two distinct pockets, with halide transfer mediated by critical lysine residue K329. Isolation of a stable intermediate following bromide oxidation (BrOx) enables single turnover catalysis in the presence of organic substrate; subsequent application of a chemoselective fluorescent probe provides "],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.10.24.684477"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12633397"],"repository":["biostudies-literature"],"pubmed_title":["Separation of halide oxidation and substrate halogenation chemistries rationalizes site-selective vanadium dependent haloperoxidase catalysis."],"pmcid":["PMC12633397"],"funding_grant_id":["R01 GM129325","R35 GM147235","U24 GM129547","R24 GM154185"],"pubmed_authors":["McKinnie SMK","Baumgartner JT","Loerch S","Varga LA","Calhoun JT","Serrao VHB"],"additional_accession":[]},"is_claimable":false,"name":"Separation of halide oxidation and substrate halogenation chemistries rationalizes site-selective vanadium dependent haloperoxidase catalysis.","description":"Vanadium-dependent haloperoxidases (VHPOs) catalyze the halogenation of organic molecules under mild aqueous conditions. Selective bacterial VHPOs exhibit exquisite regio- and enantiocontrol, however the precise mechanisms dictating selectivity have remained elusive. We have solved the single-particle cryo-electron microscopy (cryo-EM) structure of a selective bromoperoxidase from <i>Enhygromyxa salina</i> (esVHPO). Mutagenesis demonstrates that halide oxidation and substrate halogenation occur in two distinct pockets, with halide transfer mediated by critical lysine residue K329. Isolation of a stable intermediate following bromide oxidation (BrOx) enables single turnover catalysis in the presence of organic substrate; subsequent application of a chemoselective fluorescent probe provides ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-04T03:19:07.85Z","creation":"2026-06-04T03:12:25.689Z"},"accession":"S-EPMC12633397","cross_references":{"pubmed":["41280116"],"doi":["10.1101/2025.10.24.684477"]}}