Inactivation and conformational changes in methyl parathion hydrolase in 2,2,2-trifluoroethanol solutions: Inactivation kinetics and molecular dynamics simulation

摘要: Abstract Many improvements have been made in the understanding of functional and structural characteristics proteins a denaturant-based microenvironment. This study reports chemical denaturation methyl parathion hydrolase (MPH, EC 3.1.8.1) using 2,2,2-trifluoroethanol (TFE). MPH is an important enzyme that catalyzes hydrolysis organophosphorus agents. However, regulation activity changes during unfolding are not well studied, particularly for TFE unfolding. We investigated with first time. In this study, enzymatic at different concentrations were by measurements, intrinsic fluorescence 1-anilino-8-naphthalenesulfonate (ANS) emission spectral scans. The results showed inactivated dose-dependent manner. A Lineweaver–Burk plot analysis revealed type inhibition was reversible noncompetitive inhibition. Intrinsic ANS-binding induced obvious tertiary exposing hydrophobic groups. Furthermore, we conducted docking simulation between TFE. computer successfully binding structure estimated stability calculating energy (lowest energy: -3.18 kcal/mol). demonstrate can be TFE, provide new insights into mechanism TFE-induced ligand binding.