Gray Institute for Radiation Oncology & Biology, Department of Oncology, University of Oxford, Roosevelt Drive, Oxford OX3 7DQ, UK.
Bioorg Med Chem. 2012 Jul 15;20(14):4364-70. doi: 10.1016/j.bmc.2012.05.041. Epub 2012 May 24.
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.
体外研究结合分光光度法和血氧测定法以及酪氨酸酶作用产物的 HPLC/MS 分析表明，氢醌不是该酶的初级底物，但在儿茶酚、L-3,4-二羟基苯丙氨酸或 4-乙基苯酚存在下，通过氧化还原交换机制可间接氧化氢醌。在氢醌存在下形成的次级加成产物被证明可刺激而不是抑制底物氧化的动力学。
