The catalytic redox activity of prion protein-cuII is controlled by metal exchange with the ZnII-Thiolate clusters of Zn7Metallothionein-3

Gabriele Meloni, Andrea Crameri, Günter Fritz, Paul Davies, David R. Brown, Peter M. H. Kroneck, Milan Vašák

Research output: Contribution to journalArticle

14 Citations (Scopus)

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. Zn7MT-3 efficiently targets CuII bound in different coordination modes to PrP–CuII. By an unusual redox-dependent metal-swap reaction, MT-3 modulates the catalytic redox properties of PrP–CuII.
Original languageEnglish
Pages (from-to)1261-1265
JournalChemBiochem
Volume13
Issue number9
DOIs
Publication statusPublished - 18 Jun 2012

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