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

Abstract

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.

• Boroxine
• catalase
• drug research
• enzyme inhibition

Acknowledgements

We authors thank the Ministry of Science, Education and Sports of the Republic of Croatia for financial support for this study.