The autoxidation of 4-methylcatechol under quasi-physiological conditions, leading to 2-hyddroxy-5-1,4-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 al 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

RINALDI, ANDREA;CURRELI, NICOLETTA;RESCIGNO, ANTONIO;SANJUST, ENRICO
1995

Abstract

The autoxidation of 4-methylcatechol under quasi-physiological conditions, leading to 2-hyddroxy-5-1,4-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 al the active site of copper amine oxidases.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/102570
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 30
  • ???jsp.display-item.citation.isi??? 29
social impact