PMID: 3760860Jul 1, 1986Paper

X-ray absorption studies of the copper-beta domain of rat liver metallothionein

Journal of Inorganic Biochemistry
Graham N GeorgeS P Cramer

Abstract

Rat liver metallothionein contains two domains, each of which enfolds a separate metal-thiolate cluster. The binding stoichiometry of these clusters depends on the particular metal ion bound. In the aminoterminal beta domain the cluster can accommodate either three Cd(II) ions or six Cu(I) ions. The Cd ions are known to be coordinated in a tetrahedral geometry. In order to better understand the binding of Cu ions in this domain, the Cu-beta domain fragment of metallothionein was prepared and investigated by x-ray absorption spectroscopy. Quantitative analysis of the EXAFS data indicates copper-sulfur distances of 2.25 +/- 0.03 A. The EXAFS amplitudes and distance results are most consistent with trigonal coordination. A trigonal biprism is proposed for the Cu6Cys9 complex in which Cu occupies each vertex and cysteinyl sulfur bridges at each of the nine edges.

References

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Citations

Jan 1, 1991·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·O J MesnaR A Andersen
Jul 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·C T DameronD Hamer
Jan 1, 1992·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·H J HartmannU Weser
Jan 13, 2004·The Veterinary Quarterly·Th A M Elsinghorst
Nov 24, 2020·Metallomics : Integrated Biometal Science·Adyn MelenbacherMartin J Stillman
Dec 25, 2016·Redox Biology·Brendan SullivanYulia Pushkar
Apr 23, 1999·Journal of Inorganic Biochemistry·R BofillP González-Duarte
Mar 2, 1988·Biochimica Et Biophysica Acta·U Weser, H J Hartmann
Oct 1, 1986·Archives of Biochemistry and Biophysics·J Byrd, D R Winge
Apr 29, 2014·Inorganic Chemistry·Anne-Solène JullienPascale Delangle

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