21:I[432972,["/_next/static/chunks/bb923814e1f4d2e9.js","/_next/static/chunks/dd3ee9f5b7716ca6.js","/_next/static/chunks/4204a0ae82542ca8.js","/_next/static/chunks/30036bedc5269936.js","/_next/static/chunks/6e1aa89a642f40be.js","/_next/static/chunks/cd5e572bc3e4eb92.js","/_next/static/chunks/8ffd0b71567920d8.js","/_next/static/chunks/67ea6dfd21f16c5f.js","/_next/static/chunks/24eb4379f68013fd.js","/_next/static/chunks/b8cd775ffdf935bd.js","/_next/static/chunks/983103cd9eb7b428.js","/_next/static/chunks/d4ac9dcf27f6ff52.js","/_next/static/chunks/294b9525248c8e5f.js"],"default"] 22:T50d,Inorganic mercury compounds have been used in skin-lightening products since ancient times. Although a previous study demonstrated that mercury impeded the transfer of Cu²⁺ to the apotyrosinase, the effect of mercury on tyrosinase is still unclear. In the present study, the mechanism of mercury chloride (HgCl₂) induced inactivation of tyrosinase was investigated for the first time. The IC₅₀ values were 29.97 and 77.93 μmol/L for monophenolase and diphenolase, respectively. A kinetic analysis revealed that HgCl₂ inhibited tyrosinase activity in an irreversible non-competitive manner. 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. The molecular docking and further experiments demonstrated that HgCl₂ 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 HgCl₂ and tyrosinase, which provided a deep understanding of the inhibition mechanism of mercury on tyrosinase.23:T50e,Tyrosinase is the rate-limiting enzyme for controlling the production of melanin in the human body, and overproduction of melanin can lead to a variety of skin disorders. In this paper, the inhibitory kinetics of Dihydromyricetin (DHM) on tyrosinase and their binding mechanism were determined using spectroscopy, molecular docking, antioxidant assays, and chromatography. The spectroscopic results indicate that DHM reversibly inhibits tyrosinase in a mixed-type manner through a multiphase kinetic process with the IC₅₀ of 849.88 μM. It is shown that DHM has a strong ability to quench the intrinsic fluorescence of tyrosinase mainly through a static quenching procedure, suggesting that a stable DHM-tyrosinase complex is generated. Molecular docking results suggest that the dominant conformation of DHM does not directly bind to the active site of tyrosinase. Moreover, the antioxidant assays demonstrate that DHM has powerful antioxidant and reducing capacity but does not have the ability to reduce dopachrome to L-DOPA. Interestingly, the results of spectroscopy and chromatography indicate that DHM is a substrate of tyrosinase but not a suicide substrate. The possible inhibitory mechanism is proposed, which will be helpful to design and search for tyrosinase inhibitors.

#	Concept	H-Index	Publications	Citations
1	Engineering	2	2	99
2	Medicine	2	2	74
3	Biochemistry	2	2	74
4	Biomedical Engineering	2	2	99
5	Natural Sciences	1	1	49

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