Probing the molecular toxic mechanism of lead (II) ions with glutathione peroxidase 6 from Arabidopsis thaliana.

Along with non-biodegradability and accumulation in agricultural soil, lead (II) ions exert considerable harmful effects on plants even at trace amount, especially for the oxidative damages elicited by the lead ions-induced excessive reactive oxygen species (ROS). The glutathione peroxidases were reported to be correspondent with the oxidative stress induced by heavy metals. However, limited data are available about the potential hazardous mechanisms of the lead ions-induced oxidative damage to plants at molecular level. In this study, the harmful impacts of lead ions on Arabidopsis thaliana glutathione peroxidase 6 (AtGPX6) were assessed based on multi-spectroscopic measurements and molecular docking study. The characteristic fluorescence of AtGPX6 was quenched by lead ions with static mechanism at different temperatures. AtGPX6 exhibits a single binding site with lead ions, and then the complex formation was mainly driven by hydrogen bonding interaction and van der Waals forces on account of the negative ΔH and ΔS. The secondary structural changes were observed from the synchronous fluorescence, UV-visible absorption and Circular dichroism spectra, which led to loosen and unfold of the protein framework accompanied by the incremental hydrophobicity around the vicinity of the tryptophan residues. Therefore, this work illustrates the detailed binding mode between lead (II) ions and glutathione peroxidase 6 from Arabidopsis thaliana and the toxic effects on antioxidative defense system induced by lead ions at molecular level.