A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K₂[B₃O₃F₄OH].

In the development of boronic acid-based enzyme inhibitors as potential pharmaceutical drugs, dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH] was listed as a promising new therapeutic for treatment of these diseases. The catalase-mediated conversion of hydrogen peroxide, in the presence and absence of K2[B3O3F4OH] was studied. The kinetics conformed to the Michaelis-Menten model. Lineweaver-Burk plots were linear and plotted the family of straight lines intersected on the abscissa indicating non-competitive inhibition of the catalase. It appears that in the absence of inhibitor, catalase operates the best at conditions around pH 7.1 and in the presence of K2[B3O3F4OH] the optimum is around pH 6.2. The uncatalyzed reaction of hydrogen peroxide decomposition generally has a value of activation energy of 75 kJ mole(-1), whereas catalase, in the absence of inhibitor, lowers the value to 11.2 kJ mole(-1), while in the presence 69 mmoles L(-1) of K2[B3O3F4OH] it was 37.8 kJ mole(-1).