Determining mushroom tyrosinase inhibition by imidazolium ionic liquids: A spectroscopic and molecular docking study

The inhibition effects of imidazolium ionic liquids (ILs) on the enzyme kinetics of mushroom tyrosinase is reported. A simple UV-VIS spectrophotometric assay was used to measure the reaction kinetics of the reaction between mushroom tyrosinase and L-dopa. Seven different imidazolium ILs, comprised of 1-alkyl-3-methylimidazolium ([Im_n1⁺], n=2, 4, 6) cations paired with several anions that included Cl^-, [NO₃^-], methanesulfonate ([MeSO₃^-]), trifluoromethanesulfonate (or triflate, [TFMS^-]), and bis(trifluoromethylsulfonyl)imide ([Tf₂N^-]). Lineweaver-Burk plots were generated from the recovered k_cat and K_m parameters using four to six substrate concentrations per measurement. The results show that mushroom tyrosinase activity was consistently inhibited by all of the ILs and that the type of inhibition was non-competitive in nearly all cases. Only the data for [Im₂₁⁺][Tf₂N^-] suggested that the inhibition mechanism was competitive with the substrate. Molecular docking simulations were performed using AutoDock4.2 and AutoDock Vina and revealed that all cations docked in the L-dopa active site. Anions showed varied results that included locations both within and outside of the active site.