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Further investigation of the mechanism of Vitreoscilla hemoglobin (VHb) protection from oxidative stress in Escherichia coli

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Abstract

In Escherichia coli, Vitreoscilla hemoglobin (VHb) protects against oxidative stress, perhaps, in part, by oxidizing OxyR. Here this protection, specifically VHb-associated effects on superoxide dismutase (SOD) and catalase levels, was examined. Exponential or stationary phase cultures of SOD+ or SOD E. coli strains with or without VHb and oxyR antisense were treated with 2 mM hydrogen peroxide without sublethal peroxide induction, and compared to untreated control cultures. The hydrogen peroxide treatment was toxic to both SOD+ and SOD cells, but much more to SOD cells; expression of VHb in SOD+ strains enhanced this toxicity. In contrast, the presence of VHb was generally associated in the SOD+ background with a modest increase in SOD activity that was not greatly affected by oxyR antisense or peroxide treatment. In both SOD+ and SOD backgrounds, VHb was associated with higher catalase activity both in the presence and absence of peroxide. Contrary to its stimulatory effects in stationary phase, in exponential phase oxyR antisense generally decreased VHb levels.

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Abbreviations

SOD:

superoxide dismutase

VHb:

Vitreoscilla hemoglobin

WST-1:

water-soluble tetrazolium salt

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Correspondence to Meltem Yesilcimen Akbas.

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Akbas, M.Y., Doruk, T., Ozdemir, S. et al. Further investigation of the mechanism of Vitreoscilla hemoglobin (VHb) protection from oxidative stress in Escherichia coli . Biologia 66, 735–740 (2011). https://doi.org/10.2478/s11756-011-0099-x

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