The Catalytic Redox Activity of Prion Protein-CuII is Controlled by Metal Exchange with the ZnII-Thiolate Clusters of Zn7Metallothionein-3
Journal article published in 2012 by
Gabriele Meloni 
,
Andrea Crameri,
Günter Fritz,
Paul Davies,
David R. Brown,
Peter M. H. Kroneck,
Milan Vašák
,
Andrea Crameri,
Günter Fritz,
Paul Davies,
David R. Brown,
Peter M. H. Kroneck,
Milan Vašák
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Abstract
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(7) MT-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) .