X-ray absorption studies of yeast copper metallothionein

Journal Article · Wed Jun 15 00:00:00 EDT 1988 · J. Biol. Chem.; (United States)

OSTI ID:6975162

George, G N; Byrd, J; Winge, D R

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

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
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