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.
Research Article|May 01 1989
Xanthine oxidase-catalysed oxidation of paracetamol
J Van Steveninck;
J F Koster;
Biochem J (1989) 259 (3): 633-637.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
J Van Steveninck, J F Koster, T M A R Dubbelman; Xanthine oxidase-catalysed oxidation of paracetamol. Biochem J 1 May 1989; 259 (3): 633–637. doi: https://doi.org/10.1042/bj2590633
Download citation file: