title: 'Thermodynamic' mechanism of catalysis by haloperoxidases.
abstract: A novel 'thermodynamic' mechanistic rationale of haloperoxidase catalysis is based on the following two assumptions: (i) the role of enzyme consists only in the rapid equilibration between the halogen-containing species originating from halide and hydrogen peroxide; (ii) the interaction between the enzyme and organic substrate is kinetically insignificant and halogenation occurs as a result of the electrophilic attack of the active brominating (Br3-, Br2 and HBrO) or chlorinating (HCIO) species at monochlorodimedon indicative of a higher chloride 'specificity' of chloroperoxidase from C. fumago.
authors.affiliation: Department of Chemistry, M.V. Lomonosov Moscow State University, Russia.
authors.forename: A N
authors.initials: AN
authors.lastname: Shevelkova
authors.forename: Y I
authors.initials: YI
authors.lastname: Sal'nikov
authors.forename: N L
authors.initials: NL
authors.lastname: Kuz'mina
authors.forename: A D
authors.initials: AD
authors.lastname: Ryabov
mesh_terms: D002384:Catalysis; D002711:Chloride Peroxidase / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D003904:Mitosporic Fungi / Q000201:enzymology; D008962:Models, Theoretical; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity; D013816:Thermodynamics
chemical_list: D010544:Peroxidases; D002711:Chloride Peroxidase