Effects Of Isoxsuprine On The Catalytic Activity Of Catalase. Kinetics, Interaction Mechanism And Molecular Docking Approach

The side effects of Isoxsuprine (ISO) on the structure and catalytic function of bovine liver catalase (BLC) were investigated by various spectroscopic and theoretical methods. Enzyme inhibition kinetics showed that ISO inhibited catalase function by mixed-type inhibition. UV–Vis spectra, CD spectroscopy, synchronous and 3D fluorescence confirmed conformational changes in the structure of BLC in the presence of ISO. Fluorescence measurements showed that this drug quenches intrinsic fluorescence of BLC via static quenching mechanism. Thermodynamic parameters revealed that the reaction of ISO with catalase could proceed spontaneously through hydrogen bonds and Van der Waals forces. The molecular docking simulation in the well coherent with kinetics results showed that there is one binding site for ISO on BLC and this drug did not directly bind into the catalase activity site.