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-η2:η2-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 language | English (US) |
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Pages (from-to) | 9332-9333 |
Number of pages | 2 |
Journal | Journal of the American Chemical Society |
Volume | 124 |
Issue number | 32 |
DOIs | |
State | Published - Aug 14 2002 |
Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry