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 |
| Creators | Meloni, G., Crameri, A., Fritz, G., Davies, P., Brown, D. R., Kroneck, P. M. H. and Vašák, M. |
| DOI | 10.1002/cbic.201200198 |
| Departments | Faculty of Science > Biology & Biochemistry |
| Refereed | Yes |
| Status | Published |
| ID Code | 31203 |
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