Identification of Binding Sites in Copper(II)-Peptide Complexes Using Infrared Spectroscopy
Zhenghangcheng Li, Xueyu Feng, Kaijun Yuan, Xin‐Xing Zhang
Abstract
Complex formation of the copper(II) ion (Cu II ) with histidine (H) and H-containing peptides plays a crucial role in various metallo-enzymatic reactions. To elucidate the nature of coordinate bonding in Cu II complexes, Fourier-transform infrared spectroscopy and 2D IR spectroscopy were employed to investigate the coordination geometries of Cu II with diglycine, l -histidylglycine (HG), glycyl- l -histidine (GH), and glycylglycyl- l -histidine. The coordination of Cu II 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 Cu II –HG complex based on these spectral features significantly differs from that of Cu II –GH, suggesting a preference of the N-terminus and the steric hindrance of the H side chain in Cu II chelation.