Abstract
Metal ions in Cd,Zn-metallothionein (MT) are ligated in 2 polynuclear clusters enfolded by separate domains (1–3). The 7 metal ions are tetrahedrally coordinated to 4 cysteine thiolates (4,5). Eight of the 20 ligating cysteines exist as bridging sulfurs in the clusters (5). Other metals with tetrahedral geometry in MT include Bi(III), Co(II), Hg(II), Ni(II), and Pb(II), but the binding stoichiometry for some of these metal-protein complexes has not been established (6–10). Ag-and Cu-MT are complexes of the protein that deviate from the usual coordination of 7 tetrahedrally bound metals/polypeptide (11–14). We reported that 11–12 Ag or Cu ions can associate with MT and that the 6 domain can coordinate 6 Cu(I) ions, unlike the 3 Zn(II) ions/0 domain in Zn-MT (13,14). The higher binding stoichiometry of Cu-MT suggests that the Cu-protein adopts a binding geometry and structural conformation distinct from that of Cd,Zn-MT.
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Winge, D.R. (1987). Copper Coordination in Metallothionein. In: Kägi, J.H.R., Kojima, Y. (eds) Metallothionein II. Experientia Supplementum, vol 52. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-6784-9_14
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DOI: https://doi.org/10.1007/978-3-0348-6784-9_14
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