Protein interactions with bivalent tin. 1. Hydrolysis and complexation of tin(II) ion with glycine

J Inorg Biochem. 1996 Apr;62(1):17-29. doi: 10.1016/0162-0134(95)00085-2.

Abstract

The complexation between tin(II) ion and glycine was studied in 0.15 mol/dm3 NaCl medium at 310 K using potentiometric glass electrode titrations. In the pH range 1.1-4.5 and concentration range of the tin(II) between 0.2 and 5.0 mmol/dm3, with variable glycine-to-tin molar ratio up to 10:1, the experimental data were explained by the formation of the following complexes and their overall stability constants: log(beta +/- sigma): Sn(HGly)+, (12.78 +/- 0.08); Sn(Gly)+, (10.02 +/- 0.07); Sn(OH)Gly, (7.34 +/- 0.03), as well as the pure hydrolytic complex Sn4(OH)2+(6), whose stability constant was determined in separate experiments and found to be -4.30 +/- 0.08, under the same experimental conditions as for complexation study. The precipitate formed in tin(II)-glycine system at pH ca. 5.0 was characterized by chemical and TG analysis, I. R. spectra, X-ray powder diffraction, and electron scanning microscopy measurements. It has been shown that the precipitate has the composition Sn(OH)Gly and crystallizes in a tetragonal system with unit cell dimensions a = b = 1.584 nm, c = 0.597 nm. The mechanism of the complex formation in solution is discussed.

MeSH terms

  • Cations, Divalent / chemistry
  • Cations, Divalent / metabolism
  • Chelating Agents / chemistry
  • Chelating Agents / metabolism
  • Glycine / chemistry
  • Glycine / metabolism*
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • In Vitro Techniques
  • Microscopy, Electron, Scanning
  • Potentiometry
  • Proteins / chemistry
  • Proteins / metabolism*
  • Protons
  • Technetium / chemistry
  • Tin / chemistry
  • Tin / metabolism*

Substances

  • Cations, Divalent
  • Chelating Agents
  • Proteins
  • Protons
  • Technetium
  • Tin
  • Glycine