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Journal of Bacteriology, October 2009, p. 6394-6400, Vol. 191, No. 20
0021-9193/09/$08.00+0 doi:10.1128/JB.00552-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Key Laboratory of Industrial Ecology and Environmental Engineering, Ministry of Education, School of Environmental and Biological Science and Technology, Dalian University of Technology, Dalian 116024, China,1 Department of Civil and Environmental Engineering, Stanford University, Stanford, California 94305-4020,2 Nanjing Institute of Geography and Limnology, Chinese Academy of Sciences, Nanjing, China3
Received 24 April 2009/ Accepted 28 July 2009
The physiological role of Escherichia coli azoreductase AzoR was studied. It was found that AzoR was capable of reducing several benzo-, naphtho-, and anthraquinone compounds, which were better substrates for AzoR than the model azo substrate methyl red. The
azoR mutant displayed reduced viability when exposed to electrophilic quinones, which are capable of depleting cellular reduced glutathione (GSH). Externally added GSH can partially restore the impaired growth of the
azoR mutant caused by 2-methylhydroquinone. The transcription of azoR was induced by electrophiles, including 2-methylhydroquinone, catechol, menadione, and diamide. A transcription start point was identified 44 bp upstream from the translation start point. These data indicated that AzoR is a quinone reductase providing resistance to thiol-specific stress caused by electrophilic quinones.
Published ahead of print on 7 August 2009.
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