A functional active-site mimic of the oxy-tyrosinase enzyme forms through self-assembly of monodentate imidazole ligands, copper(I) and oxygen at −125 °C. The fidelity of this copper–dioxygen complex to the native enzyme, its inherent stability and hydroxylation reactivity suggest that an organizational role of the protein matrix suffices to realize function.
- Cooper Citek
- Christopher T. Lyons
- T. Daniel P. Stack
