Ramsden, CA and Riley, PA (2014) Mechanistic aspects of the tyrosinase oxidation of hydroquinone. Bioorganic & Medicinal Chemistry Letters, 24 (11). 2463 - 2464. ISSN 0960-894X

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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.

Item Type: Article
Additional Information: The final published version of this article is available online at https://www.sciencedirect.com/science/article/pii/S0960894X1400345X?via%3Dihub
Uncontrolled Keywords: Hydroquinone; Tyrosinase; ortho-Quinones; para-Quinones; Tautomerism
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Divisions: Faculty of Natural Sciences > School of Physical and Geographical Sciences
Depositing User: Symplectic
Date Deposited: 09 Aug 2019 07:36
Last Modified: 09 Aug 2019 13:08
URI: https://eprints.keele.ac.uk/id/eprint/6670

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