100953-27-3Relevant academic research and scientific papers
The influence of hydroquinone on tyrosinase kinetics
Stratford, Michael R.L.,Ramsden, Christopher A.,Riley, Patrick A.
experimental part, p. 4364 - 4370 (2012/08/28)
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.
