Evaluation of aspect interaction between spermine and Bovine liver catalase (BLC): spectroscopic and simulation studies

Spermine is one of the polyamines in several living organisms such as plants, animals, some bacteria, and fungi. It contributes to cell differentiation, translation and transcription of DNA, and cell signaling. Furthermore, spermine prevents oxidative damage through interaction with oxidative metabolites and antioxidative enzymes. Thus, studying complex formation between this polyamine and antioxidative enzyme helps us understand the clear role of spermine against free radicals. Thus, catalase as the most important antioxidant enzyme against oxidative stress and hydroxyl radical was selected for our study. The conformational and functional changes of catalase were investigated with absorption and computational techniques. The absorption analysis indicated that spermine could decrease the absorption of BLC by complex formation with this enzyme and more information during conformational alterations was achieved from the fluorescence and FTIR analysis. The computational results (RMSD, Rg, and RMSF) revealed a structure with more flexibility for BLC after joining with spermine. On the other hand, the kinetic study indicated that these alterations in the BLC structure led to much activity for this enzyme.