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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1994 Feb 15;91(4):1328–1331. doi: 10.1073/pnas.91.4.1328

NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon.

S I Liochev 1, A Hausladen 1, W F Beyer Jr 1, I Fridovich 1
PMCID: PMC43151  PMID: 8108411

Abstract

Soluble extracts of Escherichia coli contain four NADPH:paraquat diaphorases that were separable by anion-exchange HPLC over Mono Q. One of these was induced when the cells were exposed to paraquat. This was the case in a soxRS-competent strain but not in a soxRS-null strain, while a soxRS-constitutive strain overexpressed this diaphorase without the stimulus of exposure to paraquat. This NADPH:paraquat diaphorase could use cytochrome c or nitroblue tetrazolium as an electron acceptor, whereas O2 was a relatively poor acceptor. This diaphorase was identified as the NADPH:ferredoxin reductase. A role for reduced ferredoxin and flavodoxin in the adaptive soxRS response to oxidative stress and in the regulation of the redox status of soxR is discussed.

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Selected References

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