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  • Title: X-ray absorption spectroscopy of cuprous-thiolate clusters in Saccharomyces cerevisiae metallothionein.
    Author: Zhang L, Pickering IJ, Winge DR, George GN.
    Journal: Chem Biodivers; 2008 Oct; 5(10):2042-2049. PubMed ID: 18972536.
    Abstract:
    Copper (Cu) metallothioneins are cuprous-thiolate proteins that contain multimetallic clusters, and are thought to have dual functions of Cu storage and Cu detoxification. We have used a combination of X-ray absorption spectroscopy (XAS) and density-functional theory (DFT) to investigate the nature of Cu binding to Saccharomyces cerevisiae metallothionein. We found that the XAS of metallothionein prepared, containing a full complement of Cu, was quantitatively consistent with the crystal structure, and that reconstitution of the apo-metallothionein with stoichiometric Cu results in the formation of a tetracopper cluster, indicating cooperative binding of the Cu ions by the metallothionein.
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