Identification of Binding Sites in Copper(II)-Peptide Complexes Using Infrared Spectroscopy.
J Phys Chem B
; 128(8): 1884-1891, 2024 Feb 29.
Article
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| MEDLINE
| ID: mdl-38378490
ABSTRACT
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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1
Base de datos:
MEDLINE
Asunto principal:
Cobre
/
Complejos de Coordinación
Idioma:
En
Revista:
J Phys Chem B
Asunto de la revista:
QUIMICA
Año:
2024
Tipo del documento:
Article