Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: Evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin

@article{Rompel1999PurificationAS,
  title={Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: Evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin},
  author={Annette Rompel and Helmut Fischer and Dirk Meiwes and Klaudia B{\"u}ldt-Karentzopoulos and Ren{\'e}e Dillinger and Felix Tuczek and Herbert Witzel and Bernt Prof. Dr. Krebs},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={1999},
  volume={4},
  pages={56-63}
}
Abstract We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39 800 Da and the mass of the Populus enzyme was determined to 56 050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectroscopic… 
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