Effects of divalent mercury on myosin structure of large yellow croaker and its binding mechanism: Multi-spectroscopies and molecular docking.

Abstract

Heavy metals have long biological half-lives and are therefore a major threat to aquatic organisms, especially fish. Divalent mercury (Hg(II)) is an important form from a toxicological viewpoint. In this paper, we studied the interaction mechanism between large yellow croaker myosin and Hg(II) by multi-spectroscopies and molecular docking. Hg(II) had a positive effect on improving the elasticity of myosin gel, and the constant increase of charge would destroy the gel. Hg(II) caused myosin to aggregate, and the protein's apparent structure rapidly increased in length. The content of α-helix obviously decreased, β-turns and β-sheet increased. The myosin and Hg(II) quenching type was static quenching. Thermodynamic analysis suggested hydrogen bonding and van der Waals forces were the main forces for the combination. The molecular docking further confirmed the mechanism of action. This study provides a theoretical guidance for the preventions and control of marine heavy metals.