Coordination to divalent cations by calcium-binding proteins studied by FTIR spectroscopy.

Masayuki Nara, Hisayuki Morii, Masaru Tanokura

Laboratory of Chemistry, College of Liberal Arts and Sciences, Tokyo Medical and Dental University, Chiba 272-0827, Japan. nara.las@tmd.ac.jp

Biochimica et biophysica acta 2013 Oct

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We review the Fourier-transform infrared (FTIR) spectroscopy of side-chain COO(-) groups of Ca(2+)-binding proteins: parvalbumins, bovine calmodulin, akazara scallop troponin C and related calcium binding proteins and peptide analogues. The COO(-) stretching vibration modes can be used to identify the coordination modes of COO(-) groups of Ca(2+)-binding proteins to metal ions: bidentate, unidentate, and pseudo-bridging. FTIR spectroscopy demonstrates that the coordination structure of Mg(2+) is distinctly different from that of Ca(2+) in the Ca(2+)-binding site in solution. The interpretation of COO(-) stretches is ensured on the basis of the spectra of calcium-binding peptide analogues. The implication of COO(-) stretches is discussed for Ca(2+)-binding proteins. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies. Copyright © 2012 Elsevier B.V. All rights reserved.

Citation

Masayuki Nara, Hisayuki Morii, Masaru Tanokura. Coordination to divalent cations by calcium-binding proteins studied by FTIR spectroscopy. Biochimica et biophysica acta. 2013 Oct;1828(10):2319-27