Infrared spectroscopic study of the metal-coordination structures of calcium-binding proteins

Biochemical and Biophysical Research Communications
Masayuki Nara, Masaru Tanokura

Abstract

Carboxylate (COO(-)) groups can coordinate to metal ions in of the following four modes: 'unidentate', 'bidentate', 'bridging' and 'pseudo-bridging' modes. COO(-) stretching frequencies provide information about the coordination modes of COO(-) groups to metal ions. We review the Fourier-transform infrared spectroscopy (FTIR) of side-chain COO(-) groups of Ca(2+)-binding proteins: pike parvalbumin pI 4.10, bovine calmodulin and Akazara scallop troponin C. FTIR spectroscopy of Akazara scallop troponin C has demonstrated that the coordination structure of Mg(2+) is distinctly different from that of Ca(2+) in the Ca(2+)-binding site. The assignments of the COO(-) antisymmetric stretch have been ensured on the basis of the spectra of calcium-binding peptide analogues. The downshift of the COO(-) antisymmetric stretching mode from 1565 cm(-1) to 1555-1540 cm(-1) upon Ca(2+) binding is a commonly observed feature of FTIR spectra for EF-hand proteins.

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Citations

Mar 28, 2012·Journal of the American Chemical Society·Takahiro HayashiPierre Moënne-Loccoz
Oct 16, 2012·Biochimica Et Biophysica Acta·Judit SomkutiLászló Smeller
Jun 6, 2012·Biochemical and Biophysical Research Communications·Daisuke SasakuraYuichi Takakuwa
Oct 28, 2016·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Ji ZhangZhenyuan Wang
Mar 17, 2018·Proceedings of the National Academy of Sciences of the United States of America·Sean C EdingtonCarlos R Baiz
Aug 2, 2019·Nanomaterials·Kevin SmithManos Gkikas
May 28, 2021·The Journal of Physical Chemistry. a·Sunayana MitraSean Garrett-Roe
Oct 15, 2019·Journal of Agricultural and Food Chemistry·Pengbo CuiNa Sun

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