Efforts to model the reactions of copper enzymes with dioxygen with low mol
ecular weight complexes have been quite successful during recent years. Gui
ded by Nature, intriguing model systems for the active sites of such protei
ns have been developed, In the course of these investigations, it has been
discovered that a whole variety of copper-dioxygen adducts form when simple
copper(I) complexes are oxidized with dioxygen. The course of these reacti
ons depends on the temperature, the Ligands present, and the solvent. The e
ffects of these parameters (especially the effect of Ligand modification) o
n the reactivity of copper(I) complexes towards dioxygen are discussed in d
etail in this review.