Glycylsarcosyl-L-histidylglycine, A peptide with a "breakpoint" in complex formation: hydrolysis of the complex [CuH-1L].
Coordination of CU(II) with glycylsarcosyl-L-histidylglycine to form the series of [CuL] and [CuH-1L] was studied potentiometrically and spectroscopically. [CuL] includes the Cu(N2O)O chromophore, in which Cu(II) coordinates with nitrogens from the terminal amino and imidazole groups and a carbonyl oxygen of the Gly-Sar bond, and shows a d-d transition band at 696 nm in the absorption spectrum and at 648 nm in the CD spectrum. The predominant species around pH 8 was [CuH-1L] with Cu(N3O) chromophore, in which Cu(II) coordinates with three nitrogens from a terminal amino, a deprotonated Sar-His peptide bond, and an imidazole of a histidyl residue, and shows the d-d transition band at 652 and 580 nm in the absorption and CD spectra, respectively. This species was hydrolyzed at the Gly-Sar peptide bond, yielding the Cu(II) complex of sarcosyl-L-histidylglycine.
Ueda
J
J
JU. National Institute of Radiological Sciences, Chiba, Japan.
Miyazaki
M
M
Matsushima
Y
Y
Hanaki
A
A
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006868:Hydrolysis; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D011199:Potentiometry; D013053:Spectrophotometry
D009842:Oligopeptides; C100657:glycyl-sarcosyl-histidyl-glycine; D003300:Copper