Differentiation of the multiple S- and N-oxide-reducing activities ofEscherichia coli |
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Authors: | D. Sambasivarao Dr. Joel H. Weiner |
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Affiliation: | (1) Department of Biochemistry, University of Alberta, T6G Edmonton, Alberta, Canada |
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Abstract: | InEscherichia coli, several terminal reductases catalyze the reduction of S- and N-oxide compounds. We have used mutants missing either the constitutive dimethylsulfoxide (DMSO) reductase,dmsABC, and/or the inducible trimethylamine N-oxide (TMAO) reductase,torA, to define the roles of each reductase. These studies indicated that the constitutive DMSO reductase can sustain growth on DMSO, TMAO, methionine sulfoxide (MetSO), and other N-oxide compounds. Only one inducible TMAO reductase is expressed inE. coli, and this enzyme sustains growth on TMAO but not DMSO or MetSO. Characterization of atorA–, dms–double mutant revealed that adenosine N-oxide (ANO) reductase is specifically required for anaerobic respiration on ANO in this mutant. |
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