The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo

FEBS Letters
Jorge Membrillo-HernándezRobert K Poole

Abstract

Purified flavohaemoglobin (HMP) of Escherichia coli reduces Fe(III) in a superoxide dismutase (SOD)-sensitive reaction, demonstrating superoxide anion generation during aerobic NADH oxidation. In vivo, sodA-lacZ fusion activity was increased 3-fold by introducing plasmid pPL341, containing the hmp gene, or by growth with paraquat. The effects were additive and SOXS-dependent. Thus HMP activity causes oxidative stress in vivo. Activities of sodA-lacZ and hmp-lacZ fusions were stimulated in a himA mutant, demonstrating repression of both promoters by integration host factor (IHF), but the effects of pPL341 on sodA-lacZ activity were not due to titration of IHF by the hmp promoter.

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Citations

Nov 15, 2005·Planta·Abir U IgamberdievRobert D Hill
Sep 2, 1998·Proceedings of the National Academy of Sciences of the United States of America·P R GardnerA L Salzman
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