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

Christopher A Ramsden, Michael R L Stratford, Patrick A Riley

Journal: Organic & biomolecular chemistry 2009;7(17):3388-90

PMID: 19675891

Full Text on Royal Society of Chemistry View on PubMed

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 Cu(0) from the active site.

Address: Lennard-Jones Laboratories, School of Physical and Geographical Sciences, Keele University, Staffordshire, ST5 5BG, UK.

DOI: 10.1039/b910500j

Link outs

Subscription / membership required

Full Text Sources:

https://doi.org/10.1039/b910500j

MeSH Terms: Catalysis, Catalytic Domain, Catechol Oxidase, Catechols, Copper, Genes, Transgenic, Suicide, Kinetics, Molecular Structure, Monophenol Monooxygenase, Oxidation-Reduction, Structure-Activity Relationship, Substrate Specificity