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Inhibitory Kinetics of a Trifluoromethyl-Containing 1,2,3-Triazole Derivative on Mushroom Tyrosinase Activity
被引:5
|作者:
Li Shu-Bai
[1
]
Nie Hua-Li
[1
]
Zhang Hai-Tao
[1
]
Xue Yong
[1
]
Chris Branford White
[2
]
Zhu Li-Min
[1
]
机构:
[1] Donghua Univ, Coll Chem Chem Engn & Biotechnol, Shanghai 201620, Peoples R China
[2] London Metropolitan Univ, Inst Hlth Res & Policy, London N7 8DB, England
基金:
中国国家自然科学基金;
关键词:
Trifluoromethyl-containing 1,2,3-triazole;
Mushroom tyrosinase;
Monophenolase;
Diphenolase;
Reversible parabolic-competitive inhibition;
Copper chelation;
MECHANISM;
MONOPHENOL;
FLAVONOLS;
SUBSTRATE;
ALCOHOLS;
CATECHIN;
ANALOGS;
BINDING;
ACIDS;
D O I:
10.3866/PKU.WHXB20100115
中图分类号:
O64 [物理化学(理论化学)、化学物理学];
学科分类号:
070304 ;
081704 ;
摘要:
In this study, we demonstrate that the trifluoromethyl-containing 1,2,3-triazole derivative (TF-TZ) inhibits mushroom tyrosinase. TF-TZ could inhibit the monophenolase and diphenolase activities and the inhibition is reversible. IC50 values of 30.4, and 34.5 mu mol.L-1 were estimated for the monophenolase activity and the diphenolase activity, respectively. TF-TZ could extend the lag period of the monophenolase activity. Kinetic analysis showed that parabolic-competitive inhibition of TF-TZ occurred on diphenolase. We proposed that two TF-TZ molecules combined with free tyrosinase to form enzyme-inhibitor complexes (El and EI2), and the inhibition constants (K-i1, for EI and K-i2 for EI2) were 76.9 and 9.71 mu mol.L-1, respectively. Moreover, the UV-Visible spectrum of a mixture of tyrosinase and TF-TZ exhibited a characteristic shoulder peak that could be assigned to chelation of TF-TZ to the active site.
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页码:215 / 220
页数:6
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