Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published June 18, 2012 | public
Journal Article

The Catalytic Redox Activity of Prion Protein–Cu^(II) is Controlled by Metal Exchange with the Zn^(II)–Thiolate Clusters of Zn_7Metallothionein-3

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_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).

Additional Information

© 2012 Wiley-VCH Verlag GmbH& Co. KGaA, Weinheim. Received: March 21, 2012. Published online on May 21, 2012. We thank Dr. Serge, Chesnov (Functional Genomics Center Zürich, Switzerland) for recording the ESI-MS spectra. The work was supported by the Forschungskredit der Universität Zürich (Switzerland) Grant 54043901 (G.M.) and Swiss National Science Foundation Grant 31003A-1118884 (M.V.).

Additional details

Created:
August 22, 2023
Modified:
October 17, 2023