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

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.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

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

doi

10.1016/j.jinorgbio.2010.03.004

subject

Has Abstract

pub_date

2010-07-01 00:00:00

pages

718-25

issue

7

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(10)00067-X

journal_volume

104

pub_type

杂志文章

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