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

Gabriele Meloni; Andrea Crameri; Günter Fritz; Paul Davies; David R. Brown; Peter M. H. Kroneck; Milan Vašák

doi:10.1002/cbic.201200198

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

Gabriele Meloni, Andrea Crameri, Günter Fritz, Paul Davies, David R. Brown, Peter M. H. Kroneck, Milan Vašák

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

19 Citations (SciVal)

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.

Original language	English
Pages (from-to)	1261-1265
Journal	ChemBiochem
Volume	13
Issue number	9
DOIs	https://doi.org/10.1002/cbic.201200198
Publication status	Published - 18 Jun 2012

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title = "The catalytic redox activity of prion protein-cuII is controlled by metal exchange with the ZnII-Thiolate clusters of Zn7Metallothionein-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. 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.",

author = "Gabriele Meloni and Andrea Crameri and G{\"u}nter Fritz and Paul Davies and Brown, \{David R.\} and Kroneck, \{Peter M. H.\} and Milan Va{\v s}{\'a}k",

year = "2012",

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doi = "10.1002/cbic.201200198",

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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 - https://www.scopus.com/pages/publications/84862311146

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 -

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

Abstract

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