X-ray absorption studies of the copper-beta domain of rat liver metallothionein

Journal Article · Tue Jul 01 00:00:00 EDT 1986 · J. Inorg. Biochem.; (United States)

DOI:https://doi.org/10.1016/0162-0134(86)80062-9· OSTI ID:6933502

George, G N; Winge, D; Stout, C D; Cramer, S P

Rat liver metallothionein contains two domains, each of which enfolds a separate metal-thiolate cluster. The binding stoichiometry of these clusters depends on the particular metal ion bound. In the aminoterminal beta domain the cluster can accommodate either three Cd(II) ions or six Cu(I) ions. The Cd ions are known to be coordinated in a tetrahedral geometry. In order to better understand the binding of Cu ions in this domain, the Cu-beta domain fragment of metallothionein was prepared and investigated by x-ray absorption spectroscopy. Quantitative analysis of the EXAFS data indicates copper-sulfur distances of 2.25 +/- 0.03 A. The EXAFS amplitudes and distance results are most consistent with trigonal coordination. A trigonal biprism is proposed for the Cu6Cys9 complex in which Cu occupies each vertex and cysteinyl sulfur bridges at each of the nine edges.

• Research Organization: Exxon Research and Engineering Co., Annandale, NJ
• OSTI ID: 6933502
• Journal Information: J. Inorg. Biochem.; (United States), Vol. 3
• Country of Publication: United States
• Language: English

Related Subjects

63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
METALLOTHIONEIN
STOICHIOMETRY
X-RAY SPECTROSCOPY
CADMIUM
CHEMICAL BONDS
COPPER
FOURIER ANALYSIS
LIVER
RATS
ANIMALS
BODY
DIGESTIVE SYSTEM
ELEMENTS
GLANDS
MAMMALS
METALLOPROTEINS
METALS
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RODENTS
SPECTROSCOPY
TRANSITION ELEMENTS
VERTEBRATES
560300* - Chemicals Metabolism & Toxicology
400101 - Activation
Nuclear Reaction
Radiometric & Radiochemical Procedures