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Trichloroethene reductive dehalogenase from Dehalococcoides ethenogenes: sequence of tceA and substrate range
J K Magnuson1, M F Romine, D R Burris
1Battelle/Pacific Northwest National Laboratory, Richland, Washington 99352, USA. jon.magnuson@pnl.gov
Applied and Environmental Microbiology
|December 1, 2000
Summary
Dehalococcoides ethenogenes uses TCE reductive dehalogenase (TCE-RDase) to break down chlorinated ethenes. This enzyme
Area of Science:
- Microbial metabolism
- Environmental microbiology
- Bioremediation
Background:
- Dehalococcoides ethenogenes is unique in its ability to completely dechlorinate chlorinated ethenes to ethene.
- TCE reductive dehalogenase (TCE-RDase) is a key enzyme in this dehalorespiration pathway.
Purpose of the Study:
- To characterize the TCE reductive dehalogenase (TCE-RDase) enzyme from Dehalococcoides ethenogenes.
- To elucidate the genetic basis and cellular localization of TCE-RDase.
Main Methods:
- Cloning and sequencing of the tceA gene using inverse PCR.
- N-terminal sequencing of the mature TCE-RDase enzyme.
- Membrane localization studies.
Main Results:
- TCE-RDase efficiently dechlorinated TCE, 1,2-dichloroethane, and 1,2-dibromoethane to ethene.
- The tceA gene sequence showed weak similarity to known proteins, with a conserved iron-sulfur cluster motif.
- TCE-RDase possesses a signal sequence targeting it to the cytoplasmic membrane exterior.
- A potential co-transcribed gene, tceB, may be involved in membrane association.
Conclusions:
- TCE-RDase is a crucial enzyme for the complete dechlorination of chlorinated ethenes by Dehalococcoides ethenogenes.
- The enzyme's unique signal sequence and membrane localization are important for its function.
- Further research into tceB may reveal additional mechanisms of enzyme regulation and function.