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.

Biophysical and Protein Chemistry Laboratory Department of Chemistry NIT Rourkela Rourkela India

CEITEC MU Masaryk University Brno Czech Republic

Center of Nanomaterials NIT Rourkela Rourkela India

Department of Science Roma Tre University Rome Italy

Korea Institute of Civil Engineering and Building Technology University of Science and Technology Goyang Republic of Korea

National Center for Biomolecular Research Faculty of Science Masaryk University Brno Czech Republic

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