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Issue 17, 2009
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The influence of catechol structure on the suicide-inactivation of tyrosinase

Christopher A. Ramsden,*a  Michael R. L. Stratfordb  and  Patrick A. Rileyc 
Author affiliations

* Corresponding authors

a Lennard-Jones Laboratories, School of Physical and Geographical Sciences, Keele University, Staffordshire, UK

b Gray Institute for Radiation Oncology & Biology, University of Oxford, Old Road Campus Research Building, Oxford, UK

c Totteridge Institute for Advanced Studies, The Grange, Grange Avenue, London, UK

Abstract

3,6-Difluorocatechol, which cannot act as a monooxygenase tyrosinase substrate, is an oxidase substrate, and, in contrast to other catechols, oxidation does not lead to suicide-inactivation, providing experimental evidence for an inactivation mechanism involving reductive elimination of Cu0 from the active site.

Graphical abstract: The influence of catechol structure on the suicide-inactivation of tyrosinase

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Publication details

The article was received on 03 Jun 2009, accepted on 30 Jun 2009 and first published on 09 Jul 2009


Article type: Communication
DOI: 10.1039/B910500J
Citation: Org. Biomol. Chem., 2009,7, 3388-3390
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    The influence of catechol structure on the suicide-inactivation of tyrosinase

    C. A. Ramsden, M. R. L. Stratford and P. A. Riley, Org. Biomol. Chem., 2009, 7, 3388
    DOI: 10.1039/B910500J

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