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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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RAMSDEN BMCLetter Revised Manuscript.docx - Published Version
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Official URL: https://www.sciencedirect.com/science/article/pii/...
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.
Item Type: | Article |
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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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