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.
MeSH terms
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Amine Oxidase (Copper-Containing) / metabolism*
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Amino Acid Sequence
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Catechols / chemistry*
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Chelating Agents
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Copper*
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Cyclic N-Oxides
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Dihydroxyphenylalanine / analogs & derivatives*
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Dihydroxyphenylalanine / biosynthesis
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Dipeptides
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Hydrogen-Ion Concentration
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Kinetics
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Models, Chemical
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Molecular Sequence Data
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Oligopeptides
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Oxidation-Reduction
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Oxygen
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Spectrophotometry
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Spin Labels
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Structure-Activity Relationship
Substances
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Catechols
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Chelating Agents
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Cyclic N-Oxides
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Dipeptides
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Oligopeptides
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Spin Labels
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4-methylcatechol
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6-hydroxydopa
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Dihydroxyphenylalanine
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Copper
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Amine Oxidase (Copper-Containing)
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Oxygen
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tempol