New copper(II) complexes including pyridine-2,5-dicarboxylic acid: synthesis, spectroscopic, thermal properties, crystal structure and how these complexes interact with purified PON 1 enzyme

Çağlar S., Dilek E., Alışır S., Çağlar B.

JOURNAL OF COORDINATION CHEMISTRY, vol.69, no.16, pp.2482-2492, 2016 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 69 Issue: 16
  • Publication Date: 2016
  • Doi Number: 10.1080/00958972.2016.1188295
  • Journal Name: JOURNAL OF COORDINATION CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.2482-2492
  • Keywords: Copper complexes, pyridine-2, 5-dicarboxylic acid, paraoxonase, enzyme inhibition, POROUS COORDINATION POLYMERS, LOW-DENSITY-LIPOPROTEIN, IN-VITRO INHIBITION, MAGNETIC-PROPERTIES, HYDROTHERMAL SYNTHESIS, PARAOXONASE FAMILY, TRANSITION-METALS, LIGANDS, PHOTOLUMINESCENCE, FRAMEWORKS
  • Ondokuz Mayıs University Affiliated: Yes

Abstract

We report the synthesis of two square-pyramidal copper(II) complexes, [Cu(2,5-pydc)(2-aepy)(H2O)]H2O, 1, and [Cu(2,5-pydc)(2-ampy)(H2O)]H2O, 2 (2-aepy=2-(aminoethyl)pyridine, 2-ampy=2-(aminomethyl)pyridine, 2,5-pydc=pyridine-2,5-dicarboxylic acid or isocinchomeronic acid). The synthesized complexes have been characterized by X-ray diffraction, FT-IR, elemental, and thermal analysis techniques. The crystal structure of 1 was established by X-ray analysis. Powder X-ray diffraction analysis showed that the complexes are pure. The inhibition of human serum paraoxonase 1 (PON 1, EC 3.1.8.1) enzyme with these complexes were investigated. We used diethyl 4-nitrophenyl phosphate as a substrate to measure the paraoxonase activity of PON 1 enzyme spectrophotometrically. Complexes 1 and 2 decreased the in vitro PON 1 activity with different inhibition mechanisms. Complexes 1 and 2 inhibited paraoxonase activity of this enzyme as competitively and noncompetitively, respectively.