Nara Masayuki, Morii Hisayuki, Tanokura Masaru
Laboratory of Chemistry, College of Liberal Arts and Sciences, Tokyo Medical and Dental University, Chiba 272-0827, Japan.
Biochim Biophys Acta. 2013 Oct;1828(10):2319-27. doi: 10.1016/j.bbamem.2012.11.025. Epub 2012 Nov 29.
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.
我们综述了钙结合蛋白（如小清蛋白、牛钙调蛋白、赤贝肌钙蛋白C以及相关钙结合蛋白和肽类似物）侧链COO(-)基团的傅里叶变换红外（FTIR）光谱。COO(-)伸缩振动模式可用于识别钙结合蛋白的COO(-)基团与金属离子的配位模式：双齿、单齿和假桥连。FTIR光谱表明，溶液中钙结合位点处Mg(2+)的配位结构与Ca(2+)明显不同。基于钙结合肽类似物的光谱确保了对COO(-)伸缩振动的解释。本文讨论了COO(-)伸缩振动对钙结合蛋白的意义。本文是名为：膜蛋白和肽研究中的FTIR的特刊的一部分。
