Title

"Direct copper(lll) formation from 02 and Cu(I) with biological histamine ligation•

Document Type

Article

Publication Date

2016

Abstract

Copper enzymes in biology are capable of dioxygen activation at mono-, bi-, and trimetallic active sites.(1) Given this diversity, defining the structure–reactivity relationships between Cu–O2 species is foundational to the understanding of critical redox transformations central to aerobic life. Synthetic systems that faithfully reproduce biological copper(I) ligation and oxygenate to discrete, characterizable species provide chemical precedents for potential reactivity operative in biological systems. While nature typically uses imidazole ligation via the histidine amino acid,(1) synthetic systems are dominated by pyridine, pyrazole, and alkylated amine ligation.(2, 3) Several studies of the direct oxygenation of copper(I) imidazole-ligated complexes suggest that μ-η2:η2-peroxodicopper(II) SP and trans-1,2-peroxodicopper(II) TP species are stabilized by imidazole subunits (Figure 1).(4-9) By comparison, direct oxygenation of copper(I) complexes with imidazole ligation to bis(μ-oxide)dicopper(III) O species or the more elusive trinuclear bis(μ3-oxide)Cu(II)2Cu(III) T species is heretofore unknown, raising the question of whether imidazole ligation is compatible with direct oxygenation to a copper(III) oxidation state.

DOI

10.1021/jacs.6b05538

Comments

Gary, J . B.; Citek, C.; Brown, T. A.; Zare, R. N.; Wasinger, E. C.; Stack, T. D. P. "Direct copper(lll) formation from 02 and Cu(I) with biological histamine ligation• J. Am. Chem. Soc. 2016, 138, 9986-9995.

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