Tyrosinase-like reactivity in a CuIII2(μ-O) 2 species

Anna Company, Sara Palavicini, Isaac Garcia-Bosch, Ruben Mas-Ballesté, Lawrence Que, Elena V. Rybak-Akimova, Luigi Casella, Xavi Ribas, Miquel Costas

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52 Scopus citations

Abstract

A study was conducted to demonstrate a bis(μ-oxo)dicopper(III) species that binds and ortho-hydroxylates phenolates for reactivity of tyrosinase. The study characterized a metastable species from the low-temperature reaction of sodium p-chloro-phenolate (p-Cl-C6H4ONa) with a bis(μ-oxo)dicopper(III) species. The study found that the addition of 10 equivalents of the sodium salt of p-chlorophenol at -90°C can cause bleaching of the spectral features. High performance liquid chromatography (HPLC) analysis showed that 4-chlorocatechol was formed in 76% yield. The study used UV/UVis monitoring for reaction in acetone to determine the initial features to the bis(μ-oxo) species and found that these features disappear after phenolate addition. The study observed that the activation parameters for the monophenolase reaction catalyzed by tyrosinase.

Original languageEnglish (US)
Pages (from-to)3535-3538
Number of pages4
JournalChemistry - A European Journal
Volume14
Issue number12
DOIs
StatePublished - Apr 18 2008

Keywords

  • Bioinorganic chemistry
  • Dicopper enzymes
  • Model compounds
  • O-O activation
  • Tyrosinase

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