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


Reference:

Meloni, G., Crameri, A., Fritz, G., Davies, P., Brown, D. R., Kroneck, P. M. H. and Vašák, M., 2012. The catalytic redox activity of prion protein-cuII is controlled by metal exchange with the ZnII-Thiolate clusters of Zn7Metallothionein-3. ChemBiochem, 13 (9), pp. 1261-1265.

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Official URL:

http://dx.doi.org/10.1002/cbic.201200198

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.

Details

Item Type Articles
CreatorsMeloni, G., Crameri, A., Fritz, G., Davies, P., Brown, D. R., Kroneck, P. M. H. and Vašák, M.
DOI10.1002/cbic.201200198
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code31203

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