Abstract
The release of intact Cu(I)8-thionein from copper-resistant copper-loaded yeast cells, strain X2180-1Aa, has been shown. This copper(I)-thiolate-rich protein was characterized and compared with the chemical and physiocochemical properties of intracellular yeast Cu-thionein. The same molecular mass and stoichiometry of 8 mol copper atoms/mol protein was found. No detectable difference between the Cu-thioneins was seen in luminescence emission, electronic absorption in the ultraviolet region, chiroptical data or amino acid composition. The importance of stable Cu(I)-thiolates in Cu-thionein as a safe vehicle for transporting copper in a non-reactive manner is confirmed.
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