Tyrosinase was found to be active in the sulfoxidation of thioanisol, producing the (R)-sulfoxide with high enantiomeric excess. The activity of the enzyme with phenolic and diphenolic substrates in a mixed aqueous Hepes buffer pH 6.8-methanol-glycerol solvent was also investigated over a range of temperatures. These experiments enabled us to deduce the thermodynamic parameters associated with substrate binding to the enzyme and the activation parameters associated with the rate determining step of the enzymatic reaction.