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J. Biol. Chem., Vol. 259, Issue 21, 12960-12963, Nov, 1984

Spectroscopic properties of the alpha fragment of metallothionein

AJ Zelazowski, JA Szymanska, AY Law and MJ Stillman

Absorption, CD, and magnetic circular dichroism spectra are reported for the alpha fragment of rat liver Cd,Zn-metallothionein (MT) 2. The CD and magnetic circular dichroism spectra of the Cd4 cluster unit are particularly well-resolved and are remarkably similar to data of the complete Cd,Zn-MT. It is suggested that the high signal intensity in the 225 nm CD band may be attributed to an interaction between a terminal amino acid residue and the Cd4 cluster. Titration experiments with CdCl2 and [Cu(CH3CN)4]+ show that while no additional Cd2+ can be bound in the presence of excess Cd2+, Cu+ does replace the bound Cd2+ in a complex reaction to form at least two species. One of these species requires the presence of both Cu+ and Cd2+, with a stoichiometry of Cu 3.0, Cd 2.5. Further, Cu+ displaces all the remaining Cd2+, and the spectra recorded now closely resemble Cu-MT formed by titration of Cd,Zn-MT with greater than 8 mol eq of Cu+.
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