Electrochemical Investigation of the Influence of K2[B3O3F4OH] on the Activity of Immobilized Superoxide Dismutase
| Autor: | Borivoj Galic, Edhem Hasković, Denis Hasković, Jelena Ostojić, Safija Herenda |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
chemistry.chemical_classification
biology Superoxide 010401 analytical chemistry Oxidoreductase enzyme kinetics boroxine derivative cyclic voltammetry chronoamperometry Substrate (chemistry) 02 engineering and technology Chronoamperometry 021001 nanoscience & nanotechnology 01 natural sciences Enzyme assay 0104 chemical sciences Superoxide dismutase chemistry.chemical_compound Non-competitive inhibition chemistry Oxidoreductase Electrochemistry biology.protein Biophysics Enzyme kinetics 0210 nano-technology |
| Zdroj: | International Journal of Electrochemical Science. :3279-3287 |
| ISSN: | 1452-3981 |
| DOI: | 10.20964/2018.04.35 |
| Popis: | It is known that oxidoreductase is responsible for the regulation of oxidative stress in organisms, and pathological changes occur within the cell in the form of accumulation or lack of superoxide and peroxide radicals if the oxidoreductase activity is disturbed. Currently, the development of drugs that target the affected cells while leaving healthy cells unaffected is of great interest. The action of potential drugs is based on the inhibition / activation of oxidoreductase. In this work, we studied the electrochemical parameters of superoxide dismutase as well as the action of the potential drug of boroxine - dipotassium trioxohydroxytetrafluorotriborate (K2[B3O3F4OH]) as a target therapeutic for enzyme activity. Electrochemical tests were carried out in a classical three-electrode system using cyclic voltammetry and chronoamperometry techniques, and the obtained results were presented in the form of the kinetic parameters with the maximum value of the current obtained when the solution was saturated with the substrate (Imax) and the Michaelis-Menten constant (Km). K2[B3O3F4OH] was proven to be a reversible inhibitor, and the obtained Imax without inhibitor value of 0.014 mM and Km = 12.09 mM. The results from the Lineweaver - Burk diagram show that the inhibition is a partial noncompetitive inhibition type. |
| Databáze: | OpenAIRE |
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