PMID:8612736

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Citation

Membrillo-Hernández, J, Ioannidis, N and Poole, RK (1996) The flavohaemoglobin (HMP) of Escherichia coli generates superoxide in vitro and causes oxidative stress in vivo. FEBS Lett. 382:141-4

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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Keywords

Aerobiosis; Bacterial Proteins/biosynthesis; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Dihydropteridine Reductase; Enzyme Induction; Escherichia coli/metabolism; Escherichia coli Proteins; Ferric Compounds/metabolism; Hemeproteins/genetics; Hemeproteins/metabolism; Integration Host Factors; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxidative Stress/physiology; Paraquat/pharmacology; Recombinant Fusion Proteins/biosynthesis; Superoxide Dismutase/biosynthesis; Superoxide Dismutase/genetics; Superoxides/metabolism; Trans-Activators; Transcription Factors/genetics; Transcription Factors/physiology; beta-Galactosidase/biosynthesis; beta-Galactosidase/genetics

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