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Expression of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter is regulated by oxygen, light intensity and availability of substrate. Since dimethylsulfoxide reductase contains a pterin molybdenum cofactor, the role of molybdate in the regulation of dor operon expression was investigated. In this report we show that the molybdate-responsive transcriptional regulator, MopB, and molybdate are essential for maximal dimethylsulfoxide reductase activity and expression of a dorA::lacZ transcriptional fusion in Rhodobacter capsulatus. In contrast, mop genes are not required for the expression of the periplasmic nitrate reductase or xanthine dehydrogenase in R. capsulatus under conditions of molybdenum sufficiency. This is the first report demonstrating a clear functional difference between the ModE homologues MopB and MopA in this bacterium. The results suggest that MopA is primarily involved in the regulation of nitrogen fixation gene expression in response to molybdate while MopB has a role in nitrogen fixation and dimethylsulfoxide respiration.
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A G McEwan
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May 1997,
European journal of biochemistry,
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September 1996,
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April 2004,
FEBS letters,
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February 2002,
Microbiology (Reading, England),
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April 1997,
The Journal of biological chemistry,
P S Solomon, and
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June 1999,
Microbiology (Reading, England),
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November 1995,
FEMS microbiology letters,
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Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,
P S Solomon, and
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W Klipp, and
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October 2008,
Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology,
