Infrared spectroscopic study of the metal-coordination structures of calcium-binding proteins
Infrared spectroscopic study of the metal-coordination structures of calcium-binding proteins
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DOI：
10.1016/j.bbrc.2007.11.188
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发表时间：
2008-04-25
影响因子：
3.1
通讯作者：
Tanokura, Masaru
中科院分区：
文献类型：
--
作者：
Nara, Masayuki;Tanokura, Masaru
羧酸根（COO-）与金属离子的配位方式有四种：“单配位”、“双配位”、“桥连”和“假桥连”。COO-伸缩频率提供了COO-基团与金属离子配位模式的信息.本文综述了梭子鱼小清蛋白p/4.10、牛钙调素和赤栉孔扇贝肌钙蛋白C等钙结合蛋白侧链COO-基团的傅里叶变换红外光谱（FTIR）研究。红外光谱分析表明，赤栉孔扇贝肌钙蛋白C的钙离子结合位点中Mg ~（2+）和Ca ~（2+）的配位结构明显不同。的COO-反对称伸缩的分配已确保钙结合肽类似物的光谱的基础上。Ca 2+结合后COO-反对称伸缩模式从1565 cm（-1）下移至1555-1540 cm（-1）是EF-手蛋白FTIR光谱的常见特征。(c)2007年爱思唯尔公司All rights reserved.
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 Ca2+-binding proteins: pike parvalbumin p/4.10, bovine calmodulin and Akazara scallop troponin C. FTIR spectroscopy of Akazara scallop troponin C has demonstrated that the coordination structure of Mg2+ is distinctly different from that of Ca2+ in the Ca2+-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 Ca2+ binding is a commonly observed feature of FTIR spectra for EF-hand proteins. (c) 2007 Elsevier Inc. All rights reserved.