title: Catecholamines oxidation by xanthine oxidase.
abstract: Dopamine and structurally related catecholamines in the presence of hydrogen peroxide are oxidized in vitro by xanthine oxidase producing the corresponding melanin pigments. The kinetic parameters of the reaction, measured as aminochrome formation, have been calculated. The rate of peroxidation depends on enzyme and hydrogen peroxide concentration. The optimum pH for the peroxidative activity of the enzyme is around 8.5. Activation of the peroxidative reaction is also elicited by catechol compounds through a redox cycle mechanism. Implications about the possible biochemical relevance of xanthine oxidase activity on catecholamines oxidation are discussed.
authors.affiliation: CNR Center of Molecular Biology, University of Rome, La Sapienza, Italy.
authors.forename: C
authors.initials: C
authors.lastname: Foppoli
authors.forename: R
authors.initials: R
authors.lastname: Coccia
authors.forename: C
authors.initials: C
authors.lastname: Cini
authors.forename: M A
authors.initials: MA
authors.lastname: Rosei
mesh_terms: D002395:Catecholamines / Q000378:metabolism*; D004295:Dihydroxyphenylalanine / Q000378:metabolism; D006861:Hydrogen Peroxide; D045563:Indolequinones; D007211:Indoles / Q000378:metabolism; D007700:Kinetics; D010084:Oxidation-Reduction; D014969:Xanthine Oxidase / Q000378:metabolism*
chemical_list: D002395:Catecholamines; D045563:Indolequinones; D007211:Indoles; C091584:aminochrome 1; D004295:Dihydroxyphenylalanine; D006861:Hydrogen Peroxide; D014969:Xanthine Oxidase