X-Ray Absorption Spectroscopy of Cuprous-Thiolate Clusters in Saccharomyces Cerevisiae Metallothionein
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.
- Research Organization:
- Stanford Linear Accelerator Center (SLAC)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC02-76SF00515
- OSTI ID:
- 953527
- Report Number(s):
- SLAC-REPRINT-2009-356
- Journal Information:
- Chem. Biodivers.5:2042,2008, Journal Name: Chem. Biodivers.5:2042,2008 Journal Issue: 10 Vol. 5; ISSN 1612-1872
- Country of Publication:
- United States
- Language:
- English
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