Oxidation of 1,3,4,5-tetrahydro-2H-1,5-benzodiazepine oximes catalysed by
horseradish peroxidase (HRP) and recombinant Coprinus cinereus peroxidase
(rCiP) was studied spectrophotometrically. The reaction rate dependences on
the substrate and hydrogen peroxide concentrations were investigated; the
values of apparent KM and Vmax, catalytic, oxidation and reduction constants
(kcat, kox and kred, respectively) were calculated. The reactivity constants
for the reactions catalysed by rCiP were higher than those for the HRP.
Since oximes can have different structures depending on pH, the influence of
pH on the rate of oxidation of compounds was studied. The dependences of the
oxidation rate of the investigated oximes on the pH of the buffer solution
were determined, and the pKa values of the amino acids of peroxidases
responsible for the rate of catalysis were obtained. The HRP activity
dependence on pH has a classical bell-shaped character, while rCiP
dependence has a complex character.