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DOI: 10.5445/IR/1000046566
Originalveröffentlichung
DOI: 10.1039/C4DT03403A
Scopus
Zitationen: 3
Web of Science
Zitationen: 3

Complexation of Cm(III) with the recombinant N-lobe of human serum transferrin studied by time-resolved laser fluorescence spectroscopy (TRLFS)

Bauer, N.; Smith, V. C.; MacGillivray, R. T. A.; Panak, P. J.

Abstract:
The complexation of Cm(III) with the recombinant N-lobe of human serum transferrin (hTf/2N) is investigated in the pH range from 4.0 to 11.0 using TRLFS. At pH [greater-than-or-equal] 7.4 a Cm(III) hTf/2N species is formed with Cm(III) bound at the Fe(III) binding site. The results are compared with Cm(III) transferrin interaction at the C-lobe and indicate the similarity of the coordination environment of the C- and N-terminal binding sites with four amino acid residues of the protein, two H2O molecules and three additional ligands (e.g. synergistic anions such as carbonate) in the first coordination sphere. Measurements at c(carbonate)tot = 0.23 mM (ambient carbonate concentration) and c(carbonate)tot = 25 mM (physiological carbonate concentration) show that an increase of the total carbonate concentration suppresses the formation of the Cm(III) hTf/2N species significantly. Additionally, the three Cm(III) carbonate species Cm(CO3)+, Cm(CO3)2- and Cm(CO3)33- are formed successively with increasing pH. In general, carbonate complexation is a competing reaction for both Cm(III) complexation with transferrin and hTf/2N but the effect ... mehr


Zugehörige Institution(en) am KIT Institut für Nukleare Entsorgung (INE)
Publikationstyp Zeitschriftenaufsatz
Jahr 2015
Sprache Englisch
Identifikator ISSN: 0300-9246, 1364-5447, 1470-479X, 1472-7773, 1477-9226, 1477-9234
URN: urn:nbn:de:swb:90-465665
KITopen ID: 1000046566
HGF-Programm 32.01.04; LK 01
Erschienen in Dalton transactions
Band 44
Heft 4
Seiten 1850-1857
Bemerkung zur Veröffentlichung RSC geförderter Open Access-Artikel
Schlagworte Carbonate concentrations; Carbonate species; Coordination environment; Coordination sphere; Human serum transferrin; Synergistic anions; Time-resolved laser fluorescence spectroscopies; Trivalent actinides
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