作者:Michael R.L. Stratford、Christopher A. Ramsden、Patrick A. Riley
DOI:10.1016/j.bmc.2012.05.041
日期:2012.7
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.
在体外研究中,使用组合的分光光度法和血氧饱和度与酪氨酸酶作用的产物的HPLC / MS检查一起表明,氢醌是未用于所述酶的主要底物,但共鸣通过在任一邻苯二酚存在下的氧化还原交换机制,氧化升- 3,4-二羟基苯丙氨酸或4-乙基苯酚。在氢醌存在下形成的二级加成产物显示出刺激而不是抑制了底物氧化的动力学。