Complexation of U(VI) with highly phosphorylated protein, phosvitin A vibrational spectroscopic approach

Li, B; Raff, J; Barkleit, A; Bernhard, G; Foerstendorf, H

HERO ID

734704

Reference Type

Journal Article

Year

2010

Language

English

PMID

20385410

HERO ID 734704
In Press No
Year 2010
Title Complexation of U(VI) with highly phosphorylated protein, phosvitin A vibrational spectroscopic approach
Authors Li, B; Raff, J; Barkleit, A; Bernhard, G; Foerstendorf, H
Journal Journal of Inorganic Biochemistry
Volume 104
Issue 7
Page Numbers 718-725
Abstract The complexation of uranium(VI) to variant functional groups of the highly phosphorylated protein phosvitin in aqueous solution was investigated by attenuated total reflection Fourier transform infrared (ATR FT-IR) spectroscopy. For the verification of the affinity of the actinyl ions to carboxyl and phosphate groups of the amino acid side chains, samples with different phosphate to uranium(VI) (P/U) ratios were investigated under denaturing conditions as well as in aqueous medium. From a comparative study with other heavy metal ions, i.e. Ba(2+) and Pb(2+), a strong coordination of U(VI) to carboxyl and phosphoryl groups can be derived. Furthermore, with increasing P/U ratios, a preferential binding of U(VI) to phosphoryl groups is indicated by the spectra of the batch samples. These findings are confirmed by spectra of aqueous U(VI)-phosvitin complexes reflecting an explicit coordination of the uranyl ions to phosphate groups at a high P/U ratio. Our study provides a deeper insight into the molecular interactions between actinyl ions and protein, and can be conferred to other basic biomolecules such as polysaccharides and nucleic acids.
Doi 10.1016/j.jinorgbio.2010.03.004
Pmid 20385410
Wosid WOS:000278413700004
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:000278413700004
Is Public Yes
Language Text English
Keyword Phosvitin; Uranium(VI); Complexation; ATR FT-IR; Infrared spectroscopy
Is Qa No