Response of Catalase of the Mouse Primary Hepatocytes to Sodium Dodecylbenzenesulfonate and the Underlying Molecular Mechanisms.

This study investigated the adverse effects of sodium dodecylbenzenesulfonates (SDBS) on mouse primary hepatocytes by conducting cell viability, intracellular oxidative stress level, and catalase (CAT) activity assays. It was shown that SDBS altered CAT activities, triggered oxidative stress, and thus exhibited cytotoxicity to the hepatocytes. Both the stimulation of intracellular CAT production and the inhibition of molecular CAT activity contributed to intracellular CAT activity change. Molecular mechanisms underlying CAT activity inhibition and structural changes were explored by isothermal titration calorimetry, multispectroscopy, and molecular docking studies. SDBS binds to CAT with 8.81 ± 0.751 sites via electrostatic forces, resulting in structural changes with α-helix significantly decreasing to 9.7 ± 1.2%. SDBS could interact with HIS 74, ASN 147, and TYR 357 around the active sites as well as TRP 185, ASP 127, and GLN 167 within the substrate channel and therefore might result in the inhibition of molecular CAT activity.