Impact of chromate and dichromate on lysozyme stability: A spectroscopic and molecular docking investigation

A comparative study of interaction between chicken egg white lysozyme (Lyz) with two hexavalent chromate ions; chromate and dichromate; which are prevalently known for their toxicity, was investigated using different spectroscopic techniques along with a molecular docking study. Both steady-state and time-resolved studies revealed that the addition of chromate/dichromate is responsible for strong quenching of intrinsic fluorescence in Lyz and the quenching is caused by both static and dynamic quenching mechanisms. Different binding and thermodynamic parameters were also calculated at different temperatures from the intrinsic fluorescence of Lyz. The conformational change in Lyz and thermodynamic parameters obtained during the course of interaction with chromate/dichromate were well-supported by the molecular docking results.

Automated summary

In this study, the interaction between chicken egg white lysozyme (Lyz) and two hexavalent chromate ions, chromate and dichromate, was investigated. The results from spectroscopic techniques and molecular docking revealed that the addition of chromate/dichromate causes strong quenching of intrinsic fluorescence in Lyz, and this quenching is attributed to both static and dynamic mechanisms. The different binding and thermodynamic parameters were calculated from the intrinsic fluorescence of Lyz at different temperatures, and the conformational changes and thermodynamic parameters obtained were supported by the molecular docking results.