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.

Catecholamines oxidation by xantine oxidase / Foppoli, C.; Coccia, Raffaella; Cini, Chiara; Rosei, Maria Anna. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - 1334:(1997), pp. 200-206. [10.1016/S0304-4165(96)00093-1]

Catecholamines oxidation by xantine oxidase

COCCIA, Raffaella;CINI, Chiara;ROSEI, Maria Anna
1997

Abstract

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.
1997
01 Pubblicazione su rivista::01a Articolo in rivista
Catecholamines oxidation by xantine oxidase / Foppoli, C.; Coccia, Raffaella; Cini, Chiara; Rosei, Maria Anna. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - 1334:(1997), pp. 200-206. [10.1016/S0304-4165(96)00093-1]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/245738
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