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Structural, luminescence, and NMR studies of the reversible binding of acetate, lactate, citrate, and selected amino acids to chiral diaqua ytterbium, gadolinium, and europium complexes.

Dickins, R. S. and Aime, S. and Batsanov, A. S. and Beeby, A. and Botta, M. and Bruce, J. and Howard, J. A. K. and Love, C. S. and Parker, D. and Peacock, R. D. and Puschmann, H. (2002) 'Structural, luminescence, and NMR studies of the reversible binding of acetate, lactate, citrate, and selected amino acids to chiral diaqua ytterbium, gadolinium, and europium complexes.', Journal of the American Chemical Society., 124 (43). pp. 12697-12705.

Abstract

The nature of the ternary complexes formed in aqueous media at ambient pH on reversible binding of acetate, lactate, citrate, and selected amino acids and peptides to chiral diaqua europium, gadolinium, or ytterbium cationic complexes has been examined. Crystal structures of the chelated ytterbium acetate and lactate complexes have been defined in which the carboxylate oxygen occupies an "equatorial" site in the nine-coordinate adduct. The zwitterionic adduct of the citrate anion with [EuL1] was similar to the chelated lactate structure, with a 5-ring chelate involving the apical 3-hydroxy group and the a-carboxylate. Analysis of Eu and Yb emission CD spectra and lifetimes (H2O and D2O) for each ternary complex, in conjunction with H-1 NMR analyses of Eu/Yb systems and O-17 NMR and relaxometric studies of the Gd analogues, suggests that carbonate, oxalate, and malonate each form a chelated (q = 0) squareantiprismatic complex in which the dipolar NMR paramagnetic shift (Yb, Eu) and the emission circular polarization (g,., for Eu) are primarily determined by the polarizability of the axial ligand. The ternary complexes with hydrogen phosphate, with fluoride, and with Phe, His, and Ser at pH 6 are suggested to be monoaqua systems with Eu/Gd with an apical bound water molecule. However, for the ternary complexes of simple amino acids with [YbL1](3+), the enhanced charge demand favors a chelate structure with the amine N in an apical position. Crystal structures of the Gly and Ser adducts confirm this. In peptides and proteins (e.g. albumin) containing Glu or Asp residues, the more basic side chain carboxylate may chelate to the Ln ion, displacing both waters.

Item Type:Article
Full text:Full text not available from this repository.
Publisher Web site:http://dx.doi.org/10.1021/ja020836x
Record Created:10 May 2007
Last Modified:08 Apr 2009 16:31

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