Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli.
Deletion mutants of Escherichia coli lacking dimethyl sulfoxide (DMSO) reductase activity and consequently unable to utilize DMSO as an electron acceptor for anaerobic growth have been isolated. These mutants retained the ability to use trimethylamine N-oxide (TMAO) as an electron acceptor and the TMAO reductase activity was found to be unaltered. Heating the cell-free extract of the wild-type strain at 70 degrees C for 15 min selectively inactivated the DMSO reductase activity while the TMAO reductase activity remained unchanged for at least 1 h.
Daruwala
R
R
Department of Biological Sciences, Northern Illinois University, DeKalb 60115.
Meganathan
R
R
D000693:Anaerobiosis; D003470:Culture Media; D004926:Escherichia coli / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D005990:Glycerol / Q000378:metabolism; D007506:Iron-Sulfur Proteins; D007700:Kinetics; D008744:Methylamines / Q000378:metabolism*; D009154:Mutation; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D003470:Culture Media; D007506:Iron-Sulfur Proteins; D008744:Methylamines; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase; C005855:trimethyloxamine; D005990:Glycerol