X-ray absorption studies of the copper-beta domain of rat liver metallothionein.
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.
D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000378:metabolism*; D004577:Electron Probe Microanalysis; D005583:Fourier Analysis; D008099:Liver / Q000378:metabolism*; D008668:Metallothionein / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats
D003300:Copper; D008668:Metallothionein