Oxidation of diazinon and malathion by myeloperoxidase

The aim of the work was to investigate the in vitro oxidation of diazinon and malathion, organophosphorous pesticides (OPs) containing phosphorthioate group, catalyzed by enzyme myeloperoxidase (MPO). The oxidation was performed in the presence of hydrogen peroxide. The products were identified as oxon derivatives (phosphates), where the sulfur atom from thioate group was substituted by an oxygen atom. No hydrolysis products were detected after enzyme – induced oxidation. The oxidation efficiency was controlled using acethylcholinesterase (AChE) bioassay for determination of oxon derivatives concentration. The influence of OPs concentration, incubation time of OPs with MPO, as well as MPO concentration on the yield of oxo forms was investigated. Kinetic constants of MPO in oxidation of malathion and diazinon were estimated. The maximum concentration of oxo forms was achieved after 10 min incubation of OPs in 50 mM phosphate buffer (pH 6.0) with 100 nM MPO.

Enzymatic oxidation of organophosphate pesticides diazinon and malathion by myeloperoxidase was investigated and compared to non-enzymatic oxidation.Figure optionsDownload as PowerPoint slideHighlights
► Enzymatic oxidation of diazinon and malathion with myeloperoxidase was performed.
► Oxon derivates were identified as oxidation products.
► Kinetic data for enzymatic pesticide oxidation are offered.