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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.
Publication status:
Published

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Publisher copy:
10.1016/j.bmc.2012.05.041

Authors


Stratford, MR More by this author
Ramsden, CA More by this author
Journal:
Bioorganic and medicinal chemistry
Volume:
20
Issue:
14
Pages:
4364-4370
Publication date:
2012-07-05
DOI:
EISSN:
1464-3391
ISSN:
0968-0896
URN:
uuid:a40251f0-851c-4dfd-9ffe-606cd58bfe1b
Source identifiers:
339886
Local pid:
pubs:339886

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