Issue 17, 2009
From the journal:

Organic & Biomolecular Chemistry

The influence of catechol structure on the suicide-inactivation of tyrosinase

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

* 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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Article information

DOI
https://doi.org/10.1039/B910500J
Article type
Communication
Submitted
03 Jun 2009
Accepted
30 Jun 2009
First published
09 Jul 2009

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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