'Thermodynamic' mechanism of catalysis by haloperoxidases.
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.
Shevelkova
A N
AN
Department of Chemistry, M.V. Lomonosov Moscow State University, Russia.
Sal'nikov
Y I
YI
Kuz'mina
N L
NL
Ryabov
A D
AD
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
D010544:Peroxidases; D002711:Chloride Peroxidase