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), Journal Name: J. Biol. Chem.; (United States) Vol. 263:17; ISSN JBCHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
560300 -- Chemicals Metabolism & Toxicology
59 BASIC BIOLOGICAL SCIENCES
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ALGORITHMS
COHERENT SCATTERING
COPPER
DIFFRACTION
ELEMENTS
FUNGI
MATHEMATICAL LOGIC
METABOLISM
METALLOPROTEINS
METALLOTHIONEIN
METALS
MICROORGANISMS
MOLECULAR STRUCTURE
ORGANIC COMPOUNDS
PLANTS
PROTEINS
SACCHAROMYCES
SACCHAROMYCES CEREVISIAE
SCATTERING
TRANSITION ELEMENTS
X-RAY DIFFRACTION
YEASTS