The influence of hydroquinone on tyrosinase kinetics

被引:34
作者
Stratford, Michael R. L. [2 ]
Ramsden, Christopher A. [1 ]
Riley, Patrick A. [3 ]
机构
[1] Univ Keele, Sch Phys & Geog Sci, Lennard Jones Labs, Keele ST5 5BG, Staffs, England
[2] Univ Oxford, Dept Oncol, Gray Inst Radiat Oncol & Biol, Oxford OX3 7DQ, England
[3] Totteridge Inst Adv Studies, London N20 8AB, England
关键词
Tyrosinase; Hydroquinone; Quinone; Quintox mechanism; Oximetry; SUICIDE-INACTIVATION; MECHANISM; AUTOACTIVATION;
D O I
10.1016/j.bmc.2012.05.041
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
In vitro studies, using combined spectrophotometry and oximetry together with hplc/ms examination of the products of tyrosinase action demonstrate that hydroquinone is not a primary substrate for the enzyme but is vicariously oxidised by a redox exchange mechanism in the presence of either catechol, L-3,4-dihydroxyphenylalanine or 4-ethylphenol. Secondary addition products formed in the presence of hydroquinone are shown to stimulate, rather than inhibit, the kinetics of substrate oxidation. (C) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:4364 / 4370
页数:7
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