Reference: Zhang L, et al. (2008) X-ray absorption spectroscopy of cuprous-thiolate clusters in Saccharomyces cerevisiae metallothionein. Chem Biodivers 5(10):2042-2049

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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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Journal Article | Research Support, N.I.H., Extramural | Research Support, Non-U.S. Gov't
Authors
Zhang L, Pickering IJ, Winge DR, George GN
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