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

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 t...

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Veröffentlicht in:	Organic & biomolecular chemistry 2009-01, Vol.7 (17), p.3388-3390
Hauptverfasser:	Ramsden, Christopher A, Stratford, Michael R L, Riley, Patrick A
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalysis Catalytic Domain Catechol Oxidase - metabolism Catechols - chemistry Catechols - metabolism Copper - metabolism Genes, Transgenic, Suicide Kinetics Molecular Structure Monophenol Monooxygenase - metabolism Oxidation-Reduction Structure-Activity Relationship Substrate Specificity
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Zusammenfassung:	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.
ISSN:	1477-0520 1477-0539
DOI:	10.1039/b910500j