Differently bound copper(I) in yeast Cu8-thionein.

The reactivity of yeast Cu-thionein in the presence of the Cu(I)-chelators, bathocuproinesulphonate and cuproine, was examined to distinguish between possible differently coordinated Cu(I). Electronic absorption measurements revealed that two out of eight coppers of the protein reacted within seconds with the chelator. At the same time, the shape and magnitude of the characteristic Cotton bands attributable to the Cu(I)-thiolate chromophores remained constant. Due to the successful removal of circular dichroic silent copper, all specific theta Cu values rose by 53% of the original value. Thus, it is strongly suggested that two or more distinct types of Cu(I) ought to be present in Cu8-thionein. In the light of the many different Cu/cysteine ratios of Cu-thioneins from vertebrate and microbial origin, possible interconversion reactions of the Cu(I)-thiolate centres seem to be likely.