Open AccessProton‐Magnetic‐Resonance Study of Copper(I) Complexes with Peptides Containing Sulfhydryl and Imidazole Groups as Possible Model Ligands for Copper Proteins
Author(s) -
SUGIURA Yukio
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11755.x
Subject(s) - imidazole , histidine , chemistry , copper , peptide , copper protein , proton magnetic resonance , proton nmr , sulfur , crystallography , resonance (particle physics) , inorganic chemistry , stereochemistry , nuclear magnetic resonance , organic chemistry , enzyme , biochemistry , particle physics , physics
The copper(I) complexes of peptides containing sulfhydryl and imidazole groups have been investigated in aqueous solution by proton magnetic resonance ( 1 H NMR). The N ‐mercaptoacetyl‐ l ‐histidine coordinates through the sulfhydryl sulfur and imidazole nitrogen atoms to form the unique 1:1 Cu(I) complex species containing bridged imidazole. The sulfhydryl and imidazole groups are adequate ligands for not only Cu(II) but also Cu(I). The 1 H NMR spectra show that the peptide nitrogen group is not involved in complex formation of Cu(I) with N ‐mercaptoacetyl‐ l ‐histidine and 3‐mercaptopropionyl‐ l ‐histidine. The results have been discussed with respect to the protein ligands for ‘blue’ copper centers.