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
- Eprint ID
- 32017
- DOI
- 10.1002/cbic.201200198
- Resolver ID
- CaltechAUTHORS:20120621-143910899
- 54043901
- Forschungskredit der Universität Zürich
- 31003A-1118884
- Swiss National Science Foundation (SNSF)
- Created
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2012-06-28Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field