KINETICS STUDY OF THE OXIDATION OF 4-TERT-BUTYLPHENOL BY TYROSINASE

被引:37
作者
ROS, JR
RODRIGUEZLOPEZ, JN
VARON, R
GARCIACANOVAS, F
机构
[1] UNIV MURCIA,FAC BIOL,DEPT BIOQUIM & BIOL MOLEC A,MURCIA,SPAIN
[2] UNIV CASTILLA LA MANCHA,EU POLITECN ALBECETE,DEPT QUIM FIS,ALBACETE,SPAIN
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 222卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1994.tb18884.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The reaction between 4-tert-butylphenol (BuPhOH) and mushroom tyrosinase was investigated by following 4-tert-butyl-ortho-benzoquinone, whose high stability permits the reaction to be used as a model for the study of the monophenolase activity of tyrosinase. The system evolves to a pseudo-steady state through an induction period (tau), the pseudo-steady-state rate (V-ss) decreasing when the (BuPhOH) concentration increases. Increases in enzyme concentration result in a parabolic pattern with V-ss, while tau is shortened. The addition of increasing catalytic amounts of 4-tert-butylcatechol at the start of the reaction reduces tau until it is totally abolished, an initial burst being observed at high 6-t-butylatechol concentrations. Initial bursts are also obtained at pH 4.5 or lower, indicating a lower affinity of the met-tyrosinase or oxidized form for the monophenol at low pH. These experimental results can be explained by the reaction mechanism of tyrosinase.
引用
收藏
页码:449 / 452
页数:4
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