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The catalytic redox activity of prion protein-Cu(II) is controlled by metal exchange with the Zn(II) -thiolate clusters of Zn(7) metallothionein-3


Meloni, Gabriele; Crameri, Andrea; Fritz, Günter; Davies, Paul; Brown, David R; Kroneck, Peter M H; Vašák, Milan (2012). The catalytic redox activity of prion protein-Cu(II) is controlled by metal exchange with the Zn(II) -thiolate clusters of Zn(7) metallothionein-3. ChemBioChem, 13(9):1261-1265.

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(7) MT-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).

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(7) MT-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).

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2012
Deposited On:09 Oct 2012 12:42
Last Modified:05 Apr 2016 15:59
Publisher:Wiley-Blackwell
ISSN:1439-4227
Publisher DOI:https://doi.org/10.1002/cbic.201200198
PubMed ID:22615124

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