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Metallo-beta-lactamase and phosphotriesterase activities of some zinc(II) complexes

Umayal, Muthaiah and Mugesh, Govindasamy (2011) Metallo-beta-lactamase and phosphotriesterase activities of some zinc(II) complexes. In: Inorganica Chimica Acta, 372 (1, Sp.). pp. 353-361.

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Official URL: http://dx.doi.org/10.1016/j.ica.2011.03.064


Metallo-beta-lactamases (m beta l) and phosphotriesterase (PTE) are zinc(II) enzymes, which hydrolyze the beta-lactam antibiotics and toxic organophosphotriesters, respectively. In the present work, we have synthesized a few asymmetric phenolate-based ligands by sequential Mannich reaction and their corresponding zinc(II) complexes. These zinc(II) complexes were studied for their m beta l and PTE activities. It is shown that the zinc(II) complexes can hydrolyze oxacillin, the beta-lactam antibiotic, at much higher rates as compared to the hydrolysis of p-nitrophenyl diphenylphosphate (PNPDPP), the phosphotriester. Among the complexes studied, the binuclear asymmetric complex 1 having a water molecule coordinated to one of the zinc(II) ions exhibits much better mbl activity than the mononuclear complexes. However, the mononuclear zinc(II) complexes having labile chloride ions exhibit significant PTE activity, which can be ascribed to the replacement of chloride ions by hydroxide ions during hydrolysis reactions. (C) 2011 Elsevier B.V. All rights reserved.

Item Type: Journal Article
Publication: Inorganica Chimica Acta
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Antibiotic resistance;Asymmetric ligands;Metallo-beta-lactamase;Phosphotriesterase;Synthesis; Zinc(II) complexes
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited: 15 Jun 2011 05:45
Last Modified: 15 Jun 2011 05:45
URI: http://eprints.iisc.ac.in/id/eprint/38253

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