Complexation of U(VI) with highly phosphorylated protein, phosvitin A vibrational spectroscopic approach.
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.
Li
Bo
B
Institute of Radiochemistry, Forschungszentrum Dresden-Rossendorf, P.O. Box 510119, 01314 Dresden, Germany.
Raff
Johannes
J
Barkleit
Astrid
A
Bernhard
Gert
G
Foerstendorf
Harald
H
D001464:Barium; D001665:Binding Sites; D007854:Lead; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D010774:Phosvitin / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011489:Protein Denaturation; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D014501:Uranium / Q000737:chemistry*
D010750:Phosphoproteins; D001464:Barium; D007854:Lead; D014501:Uranium; D010774:Phosvitin