Abstract
Mammalian metallothionein is remarkable in its metal binding properties: well-characterized species exist for metal to sulfur ratios of M7S20, M12S20, and M18S20, where M = Cd(ll), Zn(ll), Hg(ll), Ag(I), Au(I), and Cu(I). Circular dichroism and luminescence spectra provide rich details of a complicated metal binding chemistry when metals are added directly to the metal free- or zinc-containing protein. CD spectral data unambiguously identify key metal to protein stoichiometric ratios that result in well-defined structures. Emission spectra in the 450-750 nm region have been reported for metallothioneins containing Ag(I), Au(I), and Cu(I). The luminescence of Cu-MT can also be detected directly from mammalian and yeast cells. Qualitative and quantitative interpretations show that the final structure adopted by Ag-MT is not the same as that formed by Cu(I) ions in Cu-MT. XAFS structural data are reported for a number of metallothioneins, including Ag12-MT and Ag17-MT. Electrospray ionization mass spectrometry provides details on the species formed when Ag(I) binds to metallothionein. Mass spectral data are reported for metal-free MT 2A and Agn-MT (n = 14-18).