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Evidence of the Indirect Formation of the Catecholic Intermediate Substrate Responsible for the Autoactivation Kinetics of Tyrosinase*
- C. Cooksey, P. Garratt, N. P. M. Smit
- Chemistry, BiologyJournal of Biological Chemistry
- 17 October 1997
The formation of the cyclic product accounts for the indefinite lag when N,N-dimethyltyramine is used as the substrate for tyrosinase in the absence of a dihydric phenol cofactor, and it is shown that the indoliumolate product is formed by cyclization of theortho-quinone, presented by pulse radiolysis studies.
Bipyridylium quaternary salts and related compounds. V. Pulse radiolysis studies of the reaction of paraquat radical with oxygen. Implications for the mode of action of bipyridyl herbicides.
Reactions of nitrogen dioxide in aqueous model systems: oxidation of tyrosine units in peptides and proteins.
A pulse radiolysis investigation of the oxidation of the melanin precursors 3,4-dihydroxyphenylalanine (dopa) and the cysteinyldopas.
Singlet oxygen quenching and the redox properties of hydroxycinnamic acids.
Quinone chemistry and melanogenesis.
Carotenoids Enhance Vitamin E Antioxidant Efficiency
Spontaneous redox reactions of dopaquinone and the balance between the eumelanic and phaeomelanic pathways.
Calculations demonstrate that, whilst similar pathways are invoked, the phaeomelanic pathway predominates in the presence of cysteine, irrespective of the availability of dopaquinone and thus independently of the rate of tyrosinase-catalysed oxidation.
Flash Photolysis and Pulse Radiolysis: Contributions to the Chemistry of Biology and Medicine
One of the best, the flash photolysis and pulse radiolysis contributions to the chemistry of biology and medicine is shown.
The mechanism of suicide-inactivation of tyrosinase: a substrate structure investigation.
- E. Land, C. A. Ramsden, P. Riley
- Biology, ChemistryThe Tohoku journal of experimental medicine
- 1 August 2007
An investigation of the tyrosinase-catalysed oxidation of a range of hydroxybenzenes which establish the structural requirements associated with inactivation and presents evidence for an inactivation mechanism based on catechol hydroxylation, with loss of one of the copper atoms at the active site.