"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
Repository Citation
Gary, J. Brannon, ""Direct copper(lll) formation from 02 and Cu(I) with biological histamine ligation•" (2016). Faculty Publications. 59.
https://scholarworks.sfasu.edu/chemistry_facultypubs/59
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.