The autoxidation of 4-methylcatechol under quasi-physiological conditions, leading to 2-hydroxy-5-methyl-1,4-benzoquinone, was investigated. The effects of pH and metal ions were examined. An electrophilic attack of dioxygen to the 4-methylcatechol monoanion to form a transient peroxo species is proposed. It was concluded that such a non-enzymic conversion is likely for this model compound and for its physiological counterpart, a specific tyrosyl residue incorporated in the protein chain at the active site of copper amine oxidases.
Autoxidation of 4-Methylcatechol: A Model for the Study of the Biosynthesis of Copper Amine Oxidases Quinonoid Cofactor
A C;Porcu;M C;
1995
Abstract
The autoxidation of 4-methylcatechol under quasi-physiological conditions, leading to 2-hydroxy-5-methyl-1,4-benzoquinone, was investigated. The effects of pH and metal ions were examined. An electrophilic attack of dioxygen to the 4-methylcatechol monoanion to form a transient peroxo species is proposed. It was concluded that such a non-enzymic conversion is likely for this model compound and for its physiological counterpart, a specific tyrosyl residue incorporated in the protein chain at the active site of copper amine oxidases.File in questo prodotto:
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