Interaction of europium and curium with alpha-amylase. Issue 21 (11th February 2016)

• Record Type: Journal Article
• Authors: Barkleit, Astrid; Heller, Anne; Ikeda-Ohno, Atsushi; Bernhard, Gert
• Is Part Of: Dalton transactions. Volume 45:Issue 21(2016)
• Page Start: 8724
• Page End: 8733
• Publication Date: 2016-02-11
• Subjects: Chemistry, Inorganic -- Periodicals; Chemistry, Physical and theoretical -- Periodicals; Chemistry, Inorganic -- Periodicals; 546.05
• DOI: 10.1039/c5dt04790k
• Languages: English
• ISSNs: 1477-9226

Abstract

Abstract : Batch sorption experiments, potentiometric and spectroscopic titration investigations revealed a fast and strong interaction of Eu(iii ) and Cm(iii ) with the digestive enzyme α-amylase. Abstract : The complexation of Eu(iii ) and Cm(iii ) with the protein α-amylase (Amy), a major enzyme in saliva and pancreatic juice, was investigated over wide ranges of pH and concentration at both ambient and physiological temperatures. Macroscopic sorption experiments demonstrated a strong and fast binding of Eu(iii ) to Amy between pH 5 and 8. The protein provides three independent, non-cooperative binding sites for Eu(iii ). The overall association constant of these three binding sites on the protein was calculated to be log K = 6.4 ± 0.1 at ambient temperature. With potentiometric titration, the averaged deprotonation constant of the carboxyl groups (the aspartic and glutamic acid residues) of Amy was determined to be p K a = 5.23 ± 0.14 at 25 °C and 5.11 ± 0.24 at 37 °C. Time-resolved laser-induced fluorescence spectroscopy (TRLFS) revealed two different species for both Eu(iii ) and Cm(iii ) with Amy. In the case of the Eu(iii ) species, the stability constants were determined to be log β 11 = 4.7 ± 0.2 and log β 13 = 12.0 ± 0.4 for Eu : Amy = 1 : 1 and 1 : 3 complexes, respectively, whereas the values for the respective Cm(iii ) species were log β 11 = 4.8 ± 0.1 and log β 13 = 12.1 ± 0.1. Furthermore, the obtained stability constants were extrapolated to infinite dilution to make our data compatible with the existing thermodynamic database.