PMID:9770277

Citation	Anjum, MF, Ioannidis, N and Poole, RK (1998) Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged oxidative stress and implications for its physiological role in Escherichia coli. FEMS Microbiol. Lett. 166:219-23
Abstract	The Escherichia coli flavohaemoglobin (Hmp) has a globin-like N-terminal domain and a ferredoxin-NADP-reductase-like C-terminal domain. We show here that purified Hmp oxidises both NADH and NADPH with Km values of 1.8 and 19.6 microM, respectively. Prolonged incubation of a hmp-lacZ fusion strain with the redox cycling agent paraquat resulted in a 28-fold induction of hmp gene expression, nearly 3-fold higher than after short periods of exposure. A strain overproducing Hmp was significantly more sensitive to paraquat than was the wild-type strain but, in vitro, purified Hmp was not an effective NADPH-paraquat diaphorase. Prolonged incubation of a wild-type strain with paraquat increased intracellular Hmp to spectrally detectable levels.
Links	PubMed
Keywords	Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Dihydropteridine Reductase; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes, Bacterial; Hemeproteins/genetics; Hemeproteins/metabolism; Lac Operon; NAD/metabolism; NADH, NADPH Oxidoreductases/genetics; NADH, NADPH Oxidoreductases/metabolism; NADP/metabolism; Oxidation-Reduction; Oxidative Stress/physiology; Paraquat/pharmacology; Promoter Regions, Genetic; Recombinant Fusion Proteins
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