Inhibition of Tyrosinase by Mercury Chloride: Spectroscopic and Docking Studies
Inorganic mercury compounds have been used in skin-lightening products since ancient times. Although a previous study demonstrated that mercury impeded the transfer of Cu to the apotyrosinase, the effect of mercury on tyrosinase is still unclear. In the present study, the mechanism of mercury chlori...
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Published in | Frontiers in pharmacology Vol. 11; p. 81 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Frontiers Media S.A
06.03.2020
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Subjects | |
Online Access | Get full text |
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Summary: | Inorganic mercury compounds have been used in skin-lightening products since ancient times. Although a previous study demonstrated that mercury impeded the transfer of Cu
to the apotyrosinase, the effect of mercury on tyrosinase is still unclear. In the present study, the mechanism of mercury chloride (HgCl
) induced inactivation of tyrosinase was investigated for the first time. The IC
values were 29.97 and 77.93 μmol/L for monophenolase and diphenolase, respectively. A kinetic analysis revealed that HgCl
inhibited tyrosinase activity in an irreversible non-competitive manner. The strong intrinsic fluorescence quenching suggested that the formation of the HgCl
-tyrosinase complex induced conformational changes of the enzyme, and HgCl
had only one single binding site or a single class of binding site on tyrosinase. The molecular docking and further experiments demonstrated that HgCl
bound to the amino residuals (His) in the catalytic center of tyrosinase. To our knowledge, these findings presented in this paper were the first evidence of the direct interactions between HgCl
and tyrosinase, which provided a deep understanding of the inhibition mechanism of mercury on tyrosinase. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 This article was submitted to Experimental Pharmacology and Drug Discovery, a section of the journal Frontiers in Pharmacology Edited by: Jamshed Iqbal, COMSATS University Islamabad, Pakistan Reviewed by: Cláudia Sirlene Oliveira, Pelé Petit Prince Research Institute, Brazil; Mohamed A. Abdelgawad, Al Jouf University, Saudi Arabia |
ISSN: | 1663-9812 1663-9812 |
DOI: | 10.3389/fphar.2020.00081 |