A kinetic and spectral study of the alkaline transitions of chloroperoxidase.
The optical spectrum of chloroperoxidase in the near ultraviolet and visible region was studied from pH 6 to 12. Chloroperoxidase undergoes a first transition which is irreversible at pH 7 and a second transition near pH 11. The second transition is reversible provided the incubation period above pH 11 is kept as short as possible. The spectral properties of the intermediates were studied in the Soret region by means of a rapid scan apparatus. The rates of the transitions were measured in a stopped-flow apparatus. The pH dependence of both the spectra and the rate constants indicate that at least three ionizations are involved in the first alkaline transition.
D000468:Alkalies; D002711:Chloride Peroxidase / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010544:Peroxidases / Q000032:analysis*; D011489:Protein Denaturation; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet
D000468:Alkalies; D010544:Peroxidases; D002711:Chloride Peroxidase