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Dechlorination of Atrazine by a Rhizobium sp. Isolate
Applied and Environmental Microbiology
|March 1, 1997
Summary
A novel Rhizobium sp. strain, PATR, effectively degrades the herbicide atrazine by converting it to hydroxyatrazine. The constitutive enzyme involved shows high sequence similarity to known atrazine chlorohydrolases.
Area of Science:
- Microbiology
- Environmental Science
- Biochemistry
Background:
- Atrazine is a widely used herbicide with environmental persistence.
- Microbial degradation offers a promising strategy for atrazine remediation.
Purpose of the Study:
- To isolate and characterize a soil bacterium capable of atrazine degradation.
- To identify and partially purify the enzyme responsible for atrazine transformation.
Main Methods:
- Isolation of Rhizobium sp. strain PATR from agricultural soil.
- Incubation of the strain with atrazine and analysis of metabolites using [(sup14)C]atrazine.
- Partial purification and characterization of the atrazine-degrading enzyme.
Main Results:
- Strain PATR rapidly consumed atrazine, producing hydroxyatrazine as the sole detected metabolite.
- No mineralization of atrazine was observed.
- The responsible enzyme, a constitutive hydrolase, consists of four 50-kDa subunits and shares 92% sequence identity with AtzA from Pseudomonas sp. strain ADP.
Conclusions:
- Rhizobium sp. strain PATR is a potent atrazine degrader.
- The identified hydrolase is a key enzyme in atrazine biodegradation.
- This finding contributes to developing bioremediation strategies for atrazine-contaminated environments.