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

Vitaliy B Borisov, Elena Forte, Albert Davletshin, Daniela Mastronicola, Paolo Sarti, Alessandro Giuffrè

Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, Moscow 119991, Russian Federation.

FEBS letters 2013 Jul 11

filter terms:

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. Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Citation

Vitaliy B Borisov, Elena Forte, Albert Davletshin, Daniela Mastronicola, Paolo Sarti, Alessandro Giuffrè. Cytochrome bd oxidase from Escherichia coli displays high catalase activity: an additional defense against oxidative stress. FEBS letters. 2013 Jul 11;587(14):2214-8