A stabilized μ-η22 peroxodicopper(II) complex with a secondary diamine ligand and its tyrosinase-like reactivity

Liviu M. Mirica, Michael Vance, Deanne Jackson Rudd, Britt Hedman, Keith O. Hodgson, Edward I. Solomon, T. D.P. Stack

Research output: Contribution to journalArticlepeer-review

Abstract

The activation of dioxygen (O2) by Cu(I) complexes is an ubiquitous process in biology and industrial applications. In tyrosinase, a binuclear copper enzyme, a μ-η22-peroxodicopper(II) species is generally accepted to be the active oxidant. Reported here is the characterization and reactivity of a stable μ-η2:η2-peroxodicopper(II) complex at -80 °C using a secondary diamine ligand, N,N′-di-tert-butyl-ethylenediamine (DBED). The spectroscopic characteristics of this complex (UV-vis, resonance Raman) prove to be strongly dependent on the counteranion employed and not on the solvent, suggesting an intimate interaction of the counteranions with the Cu-O2 cores. This interaction is also supported by solution EXAFS data. This new complex exhibits hydroxylation reactivity by converting phenolates to catechols, proving to be a functional model of tyrosinase. Additional interest in this Cu/O2 species results from the use of Cu(I)-DBED as a polymerization catalyst of phenols to polyphenylene oxide (PPO) with O2 as the terminal oxidant.

Original languageEnglish (US)
Pages (from-to)9332-9333
Number of pages2
JournalJournal of the American Chemical Society
Volume124
Issue number32
DOIs
StatePublished - Aug 14 2002
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry

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