Tyrosinase kinetics: discrimination between two models to explain the oxidation mechanism of monophenol and diphenol substrates

This publication has 66 references indexed in Scilit:

• Tyrosinase Kinetics: A Semi-quantitative Model of the Mechanism of Oxidation of Monohydric and Dihydric Phenolic Substrates—Reply
  Journal of Theoretical Biology, 2002
• ¹H NMR spectroscopy of the binuclear Cu(II) active site of Streptomyces antibioticus tyrosinase
  FEBS Letters, 1999
• Tyrosinase kinetics: failure of the auto-activation mechanism of monohydric phenol oxidation by rapid formation of a quinomethane intermediate
  Biochemical Journal, 1998
• Study of Stereospecificity in Pear and Strawberry Polyphenol Oxidases
  Journal of Agricultural and Food Chemistry, 1998
• Study of stereospecificity in mushroom tyrosinase
  Biochemical Journal, 1998
• Evidence of the Indirect Formation of the Catecholic Intermediate Substrate Responsible for the Autoactivation Kinetics of Tyrosinase
  Journal of Biological Chemistry, 1997
• The Stoichiometry of Tyrosinase-Catalyzed Oxidation of 4-Hydroxyanisole
  Free Radical Research Communications, 1988
• Kinetic study of the transient phase of a chemical reaction system coupled to an enzymatically catalyzed step
  Biophysical Chemistry, 1987
• A kinetic study of the melanization pathway between L-tyrosine and dopachrome
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1987
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976