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Metal-Organocatalyst for Detoxification of Phosphorothioate Pesticides: Demonstration of Acetylcholine Esterase Activity.
- Source :
-
Inorganic chemistry [Inorg Chem] 2019 Aug 05; Vol. 58 (15), pp. 9773-9784. Date of Electronic Publication: 2019 Jul 18. - Publication Year :
- 2019
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Abstract
- In recent years, transition metal complexes have been developed for catalytical degradation of a phosphate ester bond, particularly in RNA and DNA; however, less consideration has been given for development of complexes for the degradation of a phosphorothioate bond, as they are the foremost used pesticides in the environment and are toxic to human beings. In this context, we have developed copper complexes of benzimidazolium based ligands for catalytical degradation of a series of organophosphates (parathion, paraoxon, methyl-parathion) at ambient conditions. The copper complexes (assigned as N1 - N3 ) were characterized using single X-ray crystallography which revealed that all three complexes are mononuclear and distorted square planner in geometry. Further, the solution state studies of the prepared complexes were carried out using UV-visible absorption, fluorescence spectroscopy, and cyclic voltametry. The complexes N1 and N2 have benzimidazolium ionic liquid as base attached with two 2-mercapto-benzimidazole pods, whereas complex N3 contains a nonionic ligand. The synthesized copper complexes were evaluated for their catalytic activity for degradation of organophosphates. It is interesting that the complex containing the ionic ligand efficiently degrades phosphorothioate pesticides, whereas complex N3 was not found to be appropriate for degradation due to a weaker conversion rate. The organophosphate degradation studies were monitored by recording absorbance spectra of parathion in the presence of catalyst, i.e., copper complexes with respect to time. The parathion was hydrolyzed into para -nitrophenol and diethyl thiophosphate. Moreover, to analyze the inhibition activity of the pesticides toward acetylcholine esterase enzyme in the presence of prepared metal complexes, Ellman's assay was performed and revealed that, within 20 min, the inhibition of acetylcholine esterase enzyme decreases by up to 13%.
- Subjects :
- Acetylcholine analysis
Benzimidazoles chemistry
Catalysis
Copper chemistry
Crystallography, X-Ray
Esterases analysis
Metal-Organic Frameworks chemical synthesis
Models, Molecular
Molecular Structure
Phosphates toxicity
Acetylcholine metabolism
Esterases metabolism
Metal-Organic Frameworks chemistry
Pesticides chemistry
Pesticides toxicity
Phosphates chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-510X
- Volume :
- 58
- Issue :
- 15
- Database :
- MEDLINE
- Journal :
- Inorganic chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 31318533
- Full Text :
- https://doi.org/10.1021/acs.inorgchem.9b00770