Abstract
It is attempted to show the relationship of metallothionein to other metal-sulphur coordinated proteins. Special emphasis is placed to characterize the metal-sulphur binding in yeast copper-thionein employing optical methods and x-ray photoelectron spectrometry. The latter technique is particular suited to detect the charge of both copper and sulphur. In addition the appearance of distinct satellites in the Cu 2p-region allow the assignment of the 3 d9 electronic state.
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Supported by the Deutsche Forschungsgemeinschaft, grant No. We 401/14.
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Weser, U., Rupp, H. (1979). Copper-Thionein and Other Metal-Sulphur-Proteins. In: Kägi, J.H.R., Nordberg, M. (eds) Metallothionein. Experientia Supplementum, vol 34. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-6493-0_15
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DOI: https://doi.org/10.1007/978-3-0348-6493-0_15
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