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.
Rinaldi, A., Porcu, M., Curreli, N., Rescigno, A., Finazzi-Agró, A., Pedersen, J., et al. (1995). Autoxidation of 4-methylcatechol: a model for the study of the biosynthesis of copper amine oxidases quinonoid cofactor. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 214(2), 559-567.
Autoxidation of 4-methylcatechol: a model for the study of the biosynthesis of copper amine oxidases quinonoid cofactor
Finazzi-Agró A;Pedersen JZ;
1995-09-14
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
