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The influence of hydroquinone on tyrosinase kinetics

Abstract:
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. © 2012 Elsevier Ltd. All rights reserved.

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Publisher copy:
10.1016/j.bmc.2012.05.041

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Institution:
University of Oxford
Department:
Oxford, MSD, Oncology
Role:
Author
Journal:
Bioorganic and Medicinal Chemistry
Volume:
20
Issue:
14
Pages:
4364-4370
Publication date:
2012-07-15
DOI:
EISSN:
1464-3391
ISSN:
0968-0896
URN:
uuid:4bb01f9f-6a37-4c76-8327-e9d559206ca5
Source identifiers:
343047
Local pid:
pubs:343047

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