TY - JOUR
T1 - The catalytic redox activity of prion protein-cuII is controlled by metal exchange with the ZnII-Thiolate clusters of Zn7Metallothionein-3
AU - Meloni, Gabriele
AU - Crameri, Andrea
AU - Fritz, Günter
AU - Davies, Paul
AU - Brown, David R.
AU - Kroneck, Peter M. H.
AU - Vašák, Milan
PY - 2012/6/18
Y1 - 2012/6/18
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84862311146&partnerID=8YFLogxK
UR - http://dx.doi.org/10.1002/cbic.201200198
U2 - 10.1002/cbic.201200198
DO - 10.1002/cbic.201200198
M3 - Article
SN - 1439-4227
VL - 13
SP - 1261
EP - 1265
JO - ChemBiochem
JF - ChemBiochem
IS - 9
ER -