Structural alterations induce by Lead(II) nitrate pollutant in Bovine Liver Catalase

Catalase is an enzyme that catalyses the decomposition of Hydrogen peroxide into the water and molecular oxygen. This enzyme is important in the body's antioxidant defence. Lead is one of the most toxic and most important heavy metals. Lead poisoning is a public health problem in many areas of the world. Lead is a cumulative toxicant that affects multiple body systems and is particularly harmful to young children. In this study the effects of Lead(II) nitrate (Pb(NO3)2) on the structure of bovine liver catalase (BLC) were investigated by means of different spectroscopic (UV-Visible, FT-IR, and Fluorescence) techniques and SDS-PAGE electrophoresis. The SDS-PAGE electrophoresis results showed that the enzyme band did not change in different concentrations of Pb(NO3)2. The UV-Visible and FT-IR, fluorescence spectroscopy results showed that there is one binding site for Pb(NO3)2 and also some structural changes in enzyme happened after addition of Pb(NO3)2. Since BLC has efficient similarities with human catalase, this structrul changes could initiate harmful disease and should be used more carefully in industrial and other activities.