LAUSR

In the present study, the side effects of an anti-cancer compound of oxali-palladium on the function and structure of bovine liver catalase (BLC) were investigated using multiple spectroscopic (fluorescence, circular dichroism (CD) and UV–vis) and molecular docking methods. Results of kinetics study showed a noncompetitive inhibition of the enzyme for oxali-palladium. Addition of various concentrations of oxali-palladium caused a gradual reduction in the intrinsic fluorescence emission intensity of BLC due to quenching the fluorescence of BLC via a static type of quenching mechanism. Also addition of oxali-palladium to the enzyme led to increasing content of α-helix and decreasing of β-pleated sheet and random coil structures. The molecular docking study in well coherent with fluorescence spectroscopy illustrated that there is one binding site for oxali-palladium on bovine liver catalase. Docking results confirmed that static quenching is occurred whereas oxali-palladium is located at the distance of Foster theory. Moreover, docking examination in agreement with binding analyzing revealed electrostatic interaction is dominant driving force in oxali-palladium binding to BLC. According above results, it can be concluded that inhibition of BLC by anticancer drug of oxali-palladium increases the content of reactive oxygen species (ROS) which is one of the mechanisms of different anticancer drugs.