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

  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},
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… 
Monophenolase and catecholase activity of Aspergillus oryzae catechol oxidase: insights from hybrid QM/MM calculations.
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Purification and spectroscopic studies on catechol oxidase from lemon balm (Melissa officinalis).
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The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae
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Synthetic models of the active site of catechol oxidase: mechanistic studies.
This critical review extensively discusses the synthetic models of catechol oxidase, with a particular emphasis on the different approaches used in the literature to study the mechanism of the catalytic oxidation of the substrate (catechol) by these compounds.
A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes
A new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) is found and two new structures from two different crystals at 1.8- Å and at 2.5-Å resolutions are solved.
Isozymes of Ipomoea batatas catechol oxidase differ in catalase-like activity.
The amino acid sequences of two isozymes of catechol oxidase from sweet potatoes (Ipomoea batatas) were determined by Edman degradation of BrCN cleavage fragments of the native protein and by
Biochemical and structural characterization of tomato polyphenol oxidases provide novel insights into their substrate specificity
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Catechol oxidase and Copper(I/II) Complexes Derived from Bipyrazol Ligand: Synthesis, Molecular Structure Investigation of New Biomimetic Functional Model and Mechanistic Study
Abstract Herein, we investigate the in situ copper(I/II) complexes of pyrazole based on ligand: 5,5'-diphenyl-1H,1'H-3,3'-bipyrazole (H2L) and Its corresponding [C36H28CuN8] (CuL). Copper(I/II)
Catechol oxidase and phenoxazinone synthase mimicking activities of mononuclear Fe(III) and Co(III) complexes of amino-bis(phenolate)-based mixed ligands: Synthesis, spectral and electrochemical studies
Abstract A new class of aminophenol ligands, bis(5-(tert-butyl)-2-hydroxybenzyl)glycine (H3L1) and bis(2-hydroxy-5-methylbenzyl)glycine (H3L2) were synthesized by the Mannich reaction. The mixed


Kessissoglou DP (ed) Bioinorganic Chemistry
  • An Inorganic Perspective of Life. Kluwer,
  • 1995