title: The influence of catechol structure on the suicide-inactivation of tyrosinase.
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.
authors.affiliation: Lennard-Jones Laboratories, School of Physical and Geographical Sciences, Keele University, Staffordshire, ST5 5BG, UK.
authors.forename: Christopher A
authors.initials: CA
authors.lastname: Ramsden
authors.forename: Michael R L
authors.initials: MR
authors.lastname: Stratford
authors.forename: Patrick A
authors.initials: PA
authors.lastname: Riley
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D004156:Catechol Oxidase / Q000378:metabolism; D002396:Catechols / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000378:metabolism; D041722:Genes, Transgenic, Suicide; D007700:Kinetics; D015394:Molecular Structure; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D002396:Catechols; D003300:Copper; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase