X-ray absorption studies of yeast copper metallothionein
The local structures of the metal sites in copper metallothionein from Saccharomyces cerevisiae have been investigated by x-ray absorption spectroscopy at the copper and sulfur K edges. Analysis of the EXAFS (extended x-ray absorption fine structure) data indicates that each copper is trigonally coordinated to sulfur at a distance of 2.23 A. Cu-Cu interactions at 2.7 and 3.9 A have also been tentatively identified. Sulfur K edge data are compatible with cysteinyl thiolates bridging each of the eight Cu(I) ions. The data support a model for the copper cluster in yeast metallothionein consisting of a Cu8S12 core. EXAFS data on two specifically engineered carboxyl-terminal truncated mutants reveal that the copper coordination in the mutants is similar to that observed in the wild-type protein.
- Research Organization:
- Exxon Research and Engineering Company, Annandale, NJ (USA)
- OSTI ID:
- 6975162
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 263:17
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
COPPER
METABOLISM
METALLOTHIONEIN
MOLECULAR STRUCTURE
X-RAY DIFFRACTION
ALGORITHMS
SACCHAROMYCES CEREVISIAE
COHERENT SCATTERING
DIFFRACTION
ELEMENTS
FUNGI
MATHEMATICAL LOGIC
METALLOPROTEINS
METALS
MICROORGANISMS
ORGANIC COMPOUNDS
PLANTS
PROTEINS
SACCHAROMYCES
SCATTERING
TRANSITION ELEMENTS
YEASTS
550201* - Biochemistry- Tracer Techniques
560300 - Chemicals Metabolism & Toxicology