title: Coordination to divalent cations by calcium-binding proteins studied by FTIR spectroscopy.
abstract: 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.
authors.affiliation: Laboratory of Chemistry, College of Liberal Arts and Sciences, Tokyo Medical and Dental University, Chiba 272-0827, Japan. nara.las@tmd.ac.jp
authors.forename: Masayuki
authors.initials: M
authors.lastname: Nara
authors.forename: Hisayuki
authors.initials: H
authors.lastname: Morii
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D001665:Binding Sites; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002413:Cations, Divalent / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
chemical_list: D002135:Calcium-Binding Proteins; D002413:Cations, Divalent