Title : Inhibition of Tyrosinase by Mercury Chloride: Spectroscopic and Docking Studies.

Pub. Date : 2020

PMID : 32210794






5 Functional Relationships(s)
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1 In the present study, the mechanism of mercury chloride (HgCl2) induced inactivation of tyrosinase was investigated for the first time. Mercuric Chloride tyrosinase Homo sapiens
2 A kinetic analysis revealed that HgCl2 inhibited tyrosinase activity in an irreversible non-competitive manner. Mercuric Chloride tyrosinase Homo sapiens
3 The strong intrinsic fluorescence quenching suggested that the formation of the HgCl2-tyrosinase complex induced conformational changes of the enzyme, and HgCl2 had only one single binding site or a single class of binding site on tyrosinase. Mercuric Chloride tyrosinase Homo sapiens
4 The strong intrinsic fluorescence quenching suggested that the formation of the HgCl2-tyrosinase complex induced conformational changes of the enzyme, and HgCl2 had only one single binding site or a single class of binding site on tyrosinase. Mercuric Chloride tyrosinase Homo sapiens
5 The molecular docking and further experiments demonstrated that HgCl2 bound to the amino residuals (His) in the catalytic center of tyrosinase. Mercuric Chloride tyrosinase Homo sapiens