Investigation on uranyl interaction with bioactive ligands. Synthesis and structural studies of the uranyl complexes with glycine and N-(2-mercaptopropionyl)glycine
Date
2002Author

Rikkou, Maria P.


Terzis, Aris

Source
Radiochimica ActaVolume
90Issue
9-11Pages
549-554Google Scholar check
Keyword(s):
Metadata
Show full item recordAbstract
Three new uranium(VI) compounds have been prepared with glycine (Hgly), N-(2-mercaptopropionyl)glycine (Hmpg) and 2,2′-dithiobis(N-propionylglycine) (tpg). The crystal structure of [UO2(Hgly)2Cl2] has been solved, revealing the uranium atom to be seven-co-ordinated. The two zwitterionic glycines are coordinated to uranium atom by the carboxylate groups, one in a monodentate and the other in a bidentate mode. Solid state studies and low temperature 1H, 13C, 2D COSY and HMQC solution NMR spectra of the [UO2(mpg)(CH3COO)], show that mpg coordinates uranium atom by the carboxylate group.
Collections
Cite as
Related items
Showing items related by title, author, creator and subject.
-
Article
Substitution of serine for α1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position or amino acid specific
Pack, M. A.; Constantinou-Deltas, Constantinos D.; Kalia, K.; Nielsen, K. B.; Prockop, D. J. (1989)Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier ...
-
Article
Substitution of cysteine for glycine-α1-691 in the proα1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution
Steinmann, B.; Westerhausen, A.; Constantinou-Deltas, Constantinos D.; Superti-Furga, A.; Prockop, D. J. (1991)Skin fibroblast from a proband with lethal osteogenesis imperfecta synthesized a type I procollagen containing a cysteine residue in the α1(I) helical domain. Assay of thermal stability of the triple helix by proteinase ...
-
Article
Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: Evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta
Spotila, L. D.; Constantinou-Deltas, Constantinos D.; Sereda, L.; Ganguly, A.; Riggs, B. L.; Prockop, D. J. (1991)Mutations in the two genes for type I collagen (COL1A1 or COL1A2) cause osteogenesis imperfecta (OI), a heritable disease characterized by moderate to extreme brittleness of bone early in life. Here we show that a 52-year-old ...