title: 1H-, 13C-, and 113Cd-NMR study of the Cd(II) complex of a blocked peptide, Z-Cys-Ala-Pro-His-OMe, in organic solvents.
abstract: The Cd(II) complex of a peptide, Z-Cys-Ala-Pro-His-OMe was prepared and characterized by absorption, CD, 1H-, 13C-, and 113Cd-nmr, and nuclear Overhauser effect spectroscopy (NOESY) spectra to show the coordination of cysteine thiolate and histidine imizazole to Cd(II) ion. The NOESY spectra in dimethyl formamide showed that the cysteine residue was in proximity to the histidine residue. These results reveal the chelation of Z-Cys-Ala-Pro-His-OMe to Cd(II) ion in solution. Temperature-dependent dissociation equilibrium of histidine imidazole in solution was observed in this complex. Structural features of the chelating peptide are discussed.
authors.affiliation: Department of Macromolecular Science, Faculty of Science, Osaka University, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Zaima
authors.forename: N
authors.initials: N
authors.lastname: Ueyama
authors.forename: H
authors.initials: H
authors.lastname: Adachi
authors.forename: A
authors.initials: A
authors.lastname: Nakamura
mesh_terms: D000595:Amino Acid Sequence; D002104:Cadmium / Q000737:chemistry*; D002247:Carbon Isotopes; D002942:Circular Dichroism; D006859:Hydrogen; D007554:Isotopes; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D010944:Plants / Q000737:chemistry; D010970:Plastocyanin / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013053:Spectrophotometry; D013816:Thermodynamics
chemical_list: D002247:Carbon Isotopes; D007554:Isotopes; D009842:Oligopeptides; D002104:Cadmium; C092932:benzyloxycarbonyl-cysteinyl-alanyl-prolyl-histidine methyl ester; D006859:Hydrogen; D010970:Plastocyanin