Weser U, Hartmann H J
Anorganische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, F.R.G.
Biochim Biophys Acta. 1988 Mar 2;953(1):1-5. doi: 10.1016/0167-4838(88)90002-7.
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.
在存在铜（I）螯合剂（bathocuproinesulphonate和cuproine）的情况下，对酵母铜硫蛋白的反应性进行了检测，以区分可能不同配位的铜（I）。电子吸收测量表明，蛋白质的八个铜原子中有两个在几秒钟内与螯合剂发生反应。与此同时，归因于硫醇铜（I）发色团的特征科顿带的形状和大小保持不变。由于成功去除了圆二色性沉默铜，所有特定的θCu值均比原始值增加了53%。因此，强烈表明在Cu8-硫蛋白中应该存在两种或更多种不同类型的铜（I）。鉴于来自脊椎动物和微生物来源的铜硫蛋白有许多不同的铜/半胱氨酸比率，硫醇铜（I）中心的可能相互转化反应似乎是可能的。
