铜
红外光谱学
肽
化学
鉴定(生物学)
红外线的
光谱学
生物化学
生物
有机化学
物理
光学
植物
量子力学
作者
Zhixiong Li,Xiaohai Feng,Kaijun Yuan,Xin‐Xing Zhang
标识
DOI:10.1021/acs.jpcb.4c00029
摘要
Complex formation of the copper(II) ion (CuII) with histidine (H) and H-containing peptides plays a crucial role in various metallo-enzymatic reactions. To elucidate the nature of coordinate bonding in CuII complexes, Fourier-transform infrared spectroscopy and 2D IR spectroscopy were employed to investigate the coordination geometries of CuII with diglycine, l-histidylglycine (HG), glycyl-l-histidine (GH), and glycylglycyl-l-histidine. The coordination of CuII to different peptide groups, including the peptide N- and C-termini, the amide group, and the imidazole of the H side chain, exhibits distinct spectral features. The derived molecular structure of the CuII–HG complex based on these spectral features significantly differs from that of CuII–GH, suggesting a preference of the N-terminus and the steric hindrance of the H side chain in CuII chelation.
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