title: Xanthine oxidase-catalysed oxidation of paracetamol.
abstract: Paracetamol was polymerized in a reaction mixture containing xanthine oxidase, xanthine and paracetamol. This polymerization reaction was not inhibited by allopurinol or KCN, indicating that neither the molybdenum sites nor the iron-sulphur centres of the enzyme were involved in this catalytic activity. Removal of the flavin centres from the enzyme, however, completely abolished paracetamol oxidation. Spectroscopic measurements suggested that in the simultaneous presence of both paracetamol and H2O2 a peroxyflavin intermediate was formed, which is presumably responsible for the paracetamol polymerization reaction.
authors.affiliation: Department of Medical Biochemistry, Sylvius Laboratories, Leiden, The Netherlands.
authors.forename: J
authors.initials: J
authors.lastname: Van Steveninck
authors.forename: J F
authors.initials: JF
authors.lastname: Koster
authors.forename: T M
authors.initials: TM
authors.lastname: Dubbelman
mesh_terms: D000082:Acetaminophen / Q000378:metabolism*; D002384:Catalysis; D006735:Horseradish Peroxidase / Q000378:metabolism; D006878:Hydroxides / Q000378:metabolism; D011108:Polymers; D014969:Xanthine Oxidase / Q000378:metabolism*
chemical_list: D006878:Hydroxides; D011108:Polymers; D000082:Acetaminophen; D006735:Horseradish Peroxidase; D014969:Xanthine Oxidase