Effects of farnesiferol A on structure and activity of bovine liver catalase: using experimental and simulation methods

Farnesiferol A as a natural sesquiterpene coumarin includes a variety range of pharmacological and biological activities. In the present study, effects of farnesiferol A onthe structure and activity of bovine liver catalase (BLC) were assessed by different spectroscopic and simulation methods. Kinetic studies showed that farnesiferol A has a significant inhibitory activity on BLC in a non-competitive manner. UV–vis absorption, CD spectroscopy, synchronous fluorescence and fluorescence spectroscopy investigations indicated conformational changes in the structure and active site of BLC in the presence of various concentrations of farnesiferol A. Fluorescence studies showed that farnesiferol A is able to quench intrinsic emission of BLC through the static type of quenching. The obtained data in the thermodynamic analyses suggested that electrostatic interactions have a major role in the binding process of farnesiferol A on BLC. Furthermore, the role of Tyr 357 residue in the mechanism of inhibition was recognized by simulation methods

کلیدواژه ها:

Catalase ، Farnesiferol A ، Non-competitive inhibition ، Simulation