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.
Original language | English (US) |
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Pages (from-to) | 2042-2049 |
Number of pages | 8 |
Journal | Chemistry and Biodiversity |
Volume | 5 |
Issue number | 10 |
DOIs | |
State | Published - 2008 |
Externally published | Yes |
ASJC Scopus subject areas
- Bioengineering
- Biochemistry
- Chemistry(all)
- Molecular Medicine
- Molecular Biology