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  • Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and o-diphenols.

Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalyzed oxidation of monophenols and o-diphenols.

Biochimica et biophysica acta (2002-05-16)
María José Peñalver, Alexander N P Hiner, José Neptuno Rodríguez-López, Francisco García-Cánovas, José Tudela
ABSTRACT

The stoichiometry of oxygen consumption during tyrosinase-catalyzed oxidation of an o-diphenol (4-tert-butylcatechol, TBC) and a monophenol (4-tert-butylphenol, TBP) has been determined. At high [substrate]/[enzyme] ratios, in the case of o-diphenols, the stoichiometry of the enzyme-catalyzed reaction was always 1 O(2)/2 o-diphenols, although if the o-quinone product was unstable, the apparent stoichiometry could tend to 1 O(2)/1 o-diphenol due to regeneration of an o-diphenol in a side reaction. In the case of monophenols, the stoichiometry could be 1 O(2)/1 monophenol or 1.5 O(2)/1 monophenol depending if the o-quinone product was stable or unstable, respectively. However, at low [substrate]/[enzyme] ratios, the oxygen/substrate stoichiometry could, even in the case where stable products are formed, be lower than 1 O(2)/2 substrates for o-diphenols or higher than 1 O(2)/1 substrate for monophenols. These data supported the mechanism proposed by Rodríguez-López et al. [J. Biol. Chem. 267 (1992) 3801-3810], in which, during hydroxylation of monophenols, tyrosinase first transformed monophenol to o-diphenol and then either catalyzed a further oxidation to form o-quinone or released it into the reaction medium. In this second case, subsequent oxidation of the o-diphenol resulted in additional oxygen consumption.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
4-tert-Butylcatechol, ≥99.0%
Sigma-Aldrich
4-tert-Butylcatechol, ≥97.0% (HPLC)
Sigma-Aldrich
4-tert-Butylcatechol, SAJ first grade, ≥98.0%