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NADPH:Ferredoxin Oxidoreductase Acts as a Paraquat Diaphoras and is a Member of the soxRS Regulon
Stefan I. Liochev, Alfred Hausladen, Wayne F. Beyer, Jr. and Irwin Fridovich
Proceedings of the National Academy of Sciences of the United States of America
Vol. 91, No. 4 (Feb. 15, 1994), pp. 1328-1331
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2364093
Page Count: 4
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1994 National Academy of Sciences