title: The intriguing enhancement of chloroperoxidase mediated one-electron oxidations by azide, a known active-site ligand.
abstract: Azide is a well-known inhibitor of heme-enzymes. Herein, we report the counter-intuitive observation that at some concentration regimes, incorporation of azide in the reaction medium enhances chloroperoxidase (CPO, a heme-enzyme) mediated one-electron abstractions from several substrates. A diffusible azidyl radical based mechanism is proposed for explaining the phenomenon. Further, it is projected that the finding could have significant impact on routine in situ or in vitro biochemistry studies involving heme-enzyme systems and azide.
authors.affiliation: Heme & Flavo Proteins Laboratory, #204 Center for Biomedical Research, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Daniel
authors.initials: D
authors.lastname: Andrew
authors.forename: Lowell
authors.initials: L
authors.lastname: Hager
authors.forename: Kelath Murali
authors.initials: KM
authors.lastname: Manoj
mesh_terms: D001386:Azides / Q000494:pharmacology*; D020134:Catalytic Domain; D002711:Chloride Peroxidase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004583:Electrons; D008024:Ligands; D010084:Oxidation-Reduction / Q000187:drug effects
chemical_list: D001386:Azides; D008024:Ligands; D002711:Chloride Peroxidase