MT3 exchanges zinc for copper

Stable Identifier
R-HSA-5662613
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
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MT3:7Zn2+ releases 3 zinc ions and binds 4 copper ions at the N-terminal beta domain (Roschitszi et al. 2003, Meloni et al. 2007, Meloni et al. 2008). By this mechanism MT3 is able to scavenge free copper ions and swap metal with an aggregated amyloid beta:copper(II) complex and a alpha-synuclein:copper(II) complex and thereby abolish production of reactive oxygen species (Meloni et al. 2008, Meloni and Vasak 2011, Pedersen et al. 2012, Luo et al. 2013). The copper ions are divalent (copper(II), Cu2+) before binding but univalent (copper(I), Cu1+) after binding (Meloni et al. 2008).

Literature References
PubMed ID Title Journal Year
18454142 Metal swap between Zn7-metallothionein-3 and amyloid-beta-Cu protects against amyloid-beta toxicity

Meloni, G, Sonois, V, Delaine, T, Guilloreau, L, Gillet, A, Teissié, J, Faller, P, Vasák, M

Nat. Chem. Biol. 2008
17389590 Redox silencing of copper in metal-linked neurodegenerative disorders: reaction of Zn7metallothionein-3 with Cu2+ ions

Meloni, G, Faller, P, Vasák, M

J. Biol. Chem. 2007
21320589 Redox activity of ?-synuclein-Cu is silenced by Zn?-metallothionein-3

Meloni, G, Vašák, M

Free Radic. Biol. Med. 2011
22283439 Rapid exchange of metal between Zn(7)-metallothionein-3 and amyloid-? peptide promotes amyloid-related structural changes

Pedersen, JT, Hureau, C, Hemmingsen, L, Heegaard, NH, Østergaard, J, Vašák, M, Faller, P

Biochemistry 2012
23086305 The molecular mechanism for human metallothionein-3 to protect against the neuronal cytotoxicity of A?(1-42) with Cu ions

Luo, Y, Xu, Y, Bao, Q, Ding, Z, Zhu, C, Huang, ZX, Tan, X

J. Biol. Inorg. Chem. 2013
12911326 Redox labile site in a Zn4 cluster of Cu4,Zn4-metallothionein-3

Roschitzki, B, Vasák, M

Biochemistry 2003
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