The Catalytic Redox Activity of Prion Protein–CuII is Controlled by Metal Exchange with the ZnII–Thiolate Clusters of Zn7Metallothionein‐3

Silencing prion: Copper-catalyzed transformations of prion protein (PrP) lead to the production of reactive oxygen species (ROS), PrP oxidation, and cleavage and aggregation in transmissible spongiphorm encephalopathies. Zn_7MT-3 efficiently targets Cu^(II) bound in different coordination modes to PrP–Cu^(II). By an unusual redox-dependent metal-swap reaction, MT-3 modulates the catalytic redox properties of PrP–Cu^(II).