Isoproterenol oxidation by tyrosinase: intermediates characterization and kinetic study.
The present work deals with isoproterenol oxidation by mushroom tyrosinase and sodium metaperiodate. Intermediates produced at short reaction time were characterized by scanning repetitive spectrophotometry and the stoichiometry of the respective aminochrome appearance was established. The oxidation pathway from isoproterenol to aminochrome is parallel to the previously proposed for L-dopa oxidation by mushroom tyrosinase, whose steps are as follow: Isoproterenol----o-quinone-H+----o-quinone----leukoaminochrome---- aminochrome. The stoichiometry for the conversion of o-quinone-H+ into the aminochrome of isoproterenol followed the equation: 2 o-quinone-H+----isoproterenol + aminochrome. The kinetics of chemical reactions that take place from the o-quinone-H+ to aminochrome has been studied as a system of various chemical reactions coupled to an enzymatic reaction (EzCC: Enzymatic-Chemical-Chemical mechanism).
D004156:Catechol Oxidase / Q000378:metabolism*; D007545:Isoproterenol / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010504:Periodic Acid; D013053:Spectrophotometry
D010504:Periodic Acid; C009288:metaperiodate; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase; D007545:Isoproterenol