Cu(I)-thionein release from copper-loaded yeast cells

Biology of Metals
K FelixU Weser

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.

References

Aug 23, 1977·Biochimica Et Biophysica Acta·U WeserG J Strobel
Mar 28, 1977·Biochimica Et Biophysica Acta·H J Hartmann, U Weser
Mar 2, 1988·Biochimica Et Biophysica Acta·U Weser, H J Hartmann
May 18, 1981·FEBS Letters·M Beltramini, K Lerch

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Citations

Jan 1, 1989·Biology of Metals·H J HartmannU Weser
Jan 1, 1990·Biology of Metals·A DesideriU Weser
Dec 23, 2004·Proceedings of the National Academy of Sciences of the United States of America·Vito CalderoneUlrich Weser
Jan 1, 1992·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·H J HartmannU Weser
Mar 1, 2012·Tuberculosis·Jennifer L Rowland, Michael Niederweis
Oct 1, 1990·Inflammation·R MieselU Weser

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