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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo. Membrillo-Hernández, J., Ioannidis, N., Poole, R.K. FEBS Lett. (1996) [Pubmed]
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