Issue 18, 2014

Interaction of Cm(iii) and Am(iii) with human serum transferrin studied by time-resolved laser fluorescence and EXAFS spectroscopy

Abstract

The complexation of Cm(III) with human serum transferrin was investigated in a pH range from 3.5 to 11.0 using time-resolved laser fluorescence spectroscopy (TRLFS). At pH ≥ 7.4 Cm(III) is incorporated at the Fe(III) binding site of transferrin whereas at lower pH a partially bound Cm(III) transferrin species is formed. At physiological temperature (310 K) at pH 7.4, about 70% of the partially bound and 30% of the incorporated Cm(III) transferrin species are present in solution. The Cm(III) results obtained by TRLFS are in very good agreement with Am(III) EXAFS results, confirming the incorporation of Am(III) at the Fe(III) binding site at pH 8.5.

Graphical abstract: Interaction of Cm(iii) and Am(iii) with human serum transferrin studied by time-resolved laser fluorescence and EXAFS spectroscopy

Article information

Article type
Paper
Submitted
29 Nov 2013
Accepted
16 Feb 2014
First published
14 Mar 2014
This article is Open Access
Creative Commons BY license

Dalton Trans., 2014,43, 6689-6700

Interaction of Cm(III) and Am(III) with human serum transferrin studied by time-resolved laser fluorescence and EXAFS spectroscopy

N. Bauer, D. R. Fröhlich and P. J. Panak, Dalton Trans., 2014, 43, 6689 DOI: 10.1039/C3DT53371A

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