The influence of hydroquinone on tyrosinase kinetics
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,...
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| Format: | Journal article |
| Language: | English |
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2012
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| _version_ | 1826271156645134336 |
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| author | Stratford, M Ramsden, C Riley, P |
| author_facet | Stratford, M Ramsden, C Riley, P |
| author_sort | Stratford, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T21:52:13Z |
| format | Journal article |
| id | oxford-uuid:4bb01f9f-6a37-4c76-8327-e9d559206ca5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:52:13Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:4bb01f9f-6a37-4c76-8327-e9d559206ca52022-03-26T15:45:00ZThe influence of hydroquinone on tyrosinase kineticsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4bb01f9f-6a37-4c76-8327-e9d559206ca5EnglishSymplectic Elements at Oxford2012Stratford, MRamsden, CRiley, PIn 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. |
| spellingShingle | Stratford, M Ramsden, C Riley, P The influence of hydroquinone on tyrosinase kinetics |
| title | The influence of hydroquinone on tyrosinase kinetics |
| title_full | The influence of hydroquinone on tyrosinase kinetics |
| title_fullStr | The influence of hydroquinone on tyrosinase kinetics |
| title_full_unstemmed | The influence of hydroquinone on tyrosinase kinetics |
| title_short | The influence of hydroquinone on tyrosinase kinetics |
| title_sort | influence of hydroquinone on tyrosinase kinetics |
| work_keys_str_mv | AT stratfordm theinfluenceofhydroquinoneontyrosinasekinetics AT ramsdenc theinfluenceofhydroquinoneontyrosinasekinetics AT rileyp theinfluenceofhydroquinoneontyrosinasekinetics AT stratfordm influenceofhydroquinoneontyrosinasekinetics AT ramsdenc influenceofhydroquinoneontyrosinasekinetics AT rileyp influenceofhydroquinoneontyrosinasekinetics |