Journal of Chemical and Pharmaceutical Research (ISSN : 0975-7384)

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Original Articles: 2014 Vol: 6 Issue: 7

Reduced Schiff base zinc complexes as proposed models of the active site of the dinuclear zinc enzyme A. Aminopeptidase

Abstract

Complexes of zinc with ligands prepared through the reduction of Schiff bases derived from salicylaldehyde and the primary aliphatic amines 1,4-diaminobutane (H2Salbn), 1,6-diaminohexane (H2Salhx), and tris(hydroxymethyl) aminomethane (H2Saltris) have been prepared and proposed as models of the active site of the zinc enzyme Aeromonas Proteolytica aminopeptidase. The complexes were characterized by 1H-NMR, FT-IR spectroscopy, and mass spectrometry. In complexes of both H2Salbn and H2Salhx, the 5-ccordinate zinc atoms are present in a N,O environment with bridging carboxylate ligands thus providing close analogues to the enzyme's active site. On the other hand, the complex of H2Saltris contains one zinc atom with an all-oxygen environment and one zinc atom bound to one N and five O atoms.