Reductive transformation of parathion and methyl parathion by Bacillus sp.
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Based on the results of phenotypic features, phylogenetic similarity of 16S rRNA gene sequences and BIOLOG test, a soil bacterium was identified as Bacillus sp. DM-1. Using either growing cells or a cell-free extract, it transformed parathion and methyl parathion to amino derivatives by reducing the nitro group. Pesticide transformation by a cell-free extract was specifically inhibited by three nitroreductase inhibitors, indicating the presence of nitroreductase activity. The nitroreductase activity was NAD(P)H-dependent, O2-insensitive, and exhibited the substrate specificity for parathion and methyl parathion. Reductive transformation significantly decreased the toxicity of pesticides.
KeywordsBacillus Methyl parathion Nitroreductase activity Parathion Reductive Transformation
This work was supported by the 863 Hi-Tech Research and Development Program of the People’s Republic of China (No. 2005AA601020).
- Goronzy T, Drzyzga O, Kahl MW, Bruns-Nagel D, Breitung J, von Loew E, Blotevogel KH (1994) Microbial degradation of explosives and related compounds. Crit Rev Microbiol 20:265–284Google Scholar
- Holt JG, Krieg NR, Sneath PH, Staley JT, Williams ST (1994) Bergey’s manual of determinative bacteriology, 9th edn. Williams and Wilkins, Baltimore, MDGoogle Scholar
- Zenno S, Koike H, Kumar AK, Jayaraman R, Tanokura M, Saigo K (1996a) Biochemical characterization of NfsA, a Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi, flavin oxidoreductase. J Bacteriol 178:4508–4514Google Scholar
- Zenno S, Koike H, Tanokura M, Saigo K (1996b) Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRaseI, the major flavin reductase in Vibrio fischeri. J Biochem 120:736–744Google Scholar