Summary
X-ray absorption spectroscopy has been applied to the in vivo examination of copper-resistant yeast cells. The in vivo structure of the metal-binding site of the accumulated copper has been compared to that of the purified yeast thionein. Analysis of the EXAFS spectra performed on intact yeast cells indicates that the accumulated copper is univalent and is exclusively coordinated to sulfur atoms at a distance of 219 pin with an average coordination number of 2. In contrast, the purified protein indicates a univalent copper trigonally coordinated to sulfur at a distance of 221 pm. These discrepancies are discussed in terms of copper location in the resistant yeast cells.
Similar content being viewed by others
References
Abrahams IL, Bremner I, Diakun GP, Garner DC, Hasnain SS, Ross I, Vasak M (1986) Structural study of the copper and zinc sites in metal lothioneins by using extended X-ray-absorption fine structure. Biochem J 236:585–589
Bordas J, Koch HJ, Hartmann HJ, Weser U (1982) Tetrahedral copper-sulphur coordination in yeast Cu-thionein an EXAFS study. FEBS Lett 140:19–21
Ecker DJ, Butt TR, Sternberg EJ, Neeper MP, Debouck C, Gorman JA, Crooke ST (1986) Yeast metallothionein function in metal detoxification. J Biol Chem 261:16895–16900
Felix K, Hartmann HJ, Weser U (1989) Cu(I)-thionein release from copper-loaded yeast cells. Biol Metals 2:50–54
Freedman HJ, Ciriolo MR, Peisach J (1989) The role of glutathione in copper metabolism and toxicity. J Biol Chem 264:5598–5605
George NG, Byrd J, Winge DR (1988) X-ray absorption studies of yeast copper metallothionein. J Biol Chem 263:8199–8203
Lee PA, Pendry JB (1975) Theory of the extended X-ray absorption fine structure. Phys Rev B 11:2795–2811
Weser U, Hartmann HJ (1984) In: Lontie R (ed) Copper proteins and copper enzymes, vol 3. CRC Press, Boca Raton, FL, pp 151–173
Weser U, Hartmann HJ (1988) Differently bound copper(I) in yeast Cu8-thionein. Biochim Biophys Acta 953:1–5
Winge DR, Nielson KB, Gray WR, Hamer DH (1985) Yeast metallothionein. Sequence and metal-binding properties. J Biol Chem 260:14464–14470
Wright CF, Hamer DH, McKenney K (1988) Autoregulation of yeast copper-metallothionein gene depends on metal binding. J Biol Chem 263:1570–1574
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Desideri, A., Hartmanna, H.J., Morante, S. et al. An EXAFS study of the copper accumulated by yeast cells. Biol Metals 3, 45–47 (1990). https://doi.org/10.1007/BF01141177
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01141177