Cu(II)–Protamine interaction. I. The formation and structure of Cu(II)–clupeine Z complexes

✍ Scribed by Arlette Garnier; Lucia Tosi; Lucienne Mosoni; Claudio Toniolo; Gian Maria Bonora; Euclear B. Paniago

• Publisher: Wiley (John Wiley & Sons)
• Year: 1981
• Tongue: English
• Weight: 672 KB
• Volume: 20
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1981.360200508

✦ Synopsis

Abstract

The formation and structure of four different Cu(II)–clupeine Z complexes have been studied using potentiometric and spectroscopic (ir and visible absorption, and CD) measurements. The results thus obtained indicate the presence of up to 8 binding sites in the pH range from 6.5 to 10.5. The spectroscopic evidence suggests that the strongest site available contains the α‐amino terminal and the adjacent peptide nitrogen, which bind to copper from pH 5 to 6.5 to form the first complex. The stability constant of this first complex has a value of (9.5 ± 0.9) × 10^3^ mol^−1^ 1. From pH 6.5 to 8.5, two intervening guanidinium nitrogens of arginine residues occupy the two other corners of the coordination square, giving rise to the second complex. The other sites potentially available from pH 6.5 to 10.5 are formed by two amino nitrogens of arginine residues and two contiguous peptide nitrogens. The first intervene up to pH 8.5, forming the third complex, and the latter from this pH to 10.5, forming the fourth complex. Although the ligands intervening at sites 2–8 appear to be the same, the sites are by no means equivalent. The spectroscopic data enable one to distinguish three different types of binding sites.