Mechanistic aspects of the tyrosinase oxidation of hydroquinone
Abstract
Contradictory reports on the behaviour of hydroquinone as a tyrosinase substrate are reconciled in terms of the ability of the initially formed ortho-quinone to tautomerise to the thermodynamically more stable para-quinone isomer. Oxidation of phenols by native tyrosinase requires activation by in situ formation of a catechol formed via an enzyme generated ortho-quinone. In the special case of hydroquinone, catechol formation is precluded by rapid tautomerisation of the ortho-quinone precursor to catechol formation.
Acceptance Date | Apr 6, 2014 |
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Publication Date | Jun 1, 2014 |
Journal | Bioorganic & Medicinal Chemistry Letters |
Print ISSN | 0960-894X |
Publisher | Elsevier |
Pages | 2463 - 2464 |
DOI | https://doi.org/10.1016/j.bmcl.2014.04.009 |
Keywords | Hydroquinone; Tyrosinase; ortho-Quinones; para-Quinones; Tautomerism |
Publisher URL | https://www.sciencedirect.com/science/article/pii/S0960894X1400345X?via%3Dihub |
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