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Journal Articles FEBS Letters Year : 2013

Cytochrome bd oxidase from Escherichia coli displays high catalase activity: an additional defense against oxidative stress.

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Abstract

Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b558, b595 and d. We found that the enzyme, as-prepared or in turnover with O2, rapidly decomposes H2O2 with formation of approximately half a mole of O2 per mole of H2O2. Such catalase activity vanishes upon cytochrome bd reduction, does not compete with the oxygen-reductase activity, is insensitive to NO, CO, antimycin-A and N-ethylmaleimide (NEM), but is inhibited by cyanide (Ki ~2.5μM) and azide. The activity, possibly associated with heme-b595, was also observed in catalase-deficient E. coli cells following cytochrome bd over-expression suggesting a protective role against oxidative stress in vivo.

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pasteur-01054294 , version 1 (05-08-2014)

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Vitaliy B Borisov, Elena Forte, Albert Davletshin, Daniela Mastronicola, Paolo Sarti, et al.. Cytochrome bd oxidase from Escherichia coli displays high catalase activity: an additional defense against oxidative stress.. FEBS Letters, 2013, 587 (14), pp.2214-8. ⟨10.1016/j.febslet.2013.05.047⟩. ⟨pasteur-01054294⟩

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