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

Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b(558), b(595) and d. We found that the enzyme, as-prepared or in turnover with O-2, rapidly decomposes H2O2 with formation of approximately half a mole of O-2 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 (K-i similar to 2.5 mu M) and azide. The activity, possibly associated with heme-b(595), was also observed in catalase-deficient E. coli cells following cytochrome bd over-expression suggesting a protective role against oxidative stress in vivo. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress / V. B., *borisov; Forte, Elena; Albert, Davletshin; Mastronicola, Daniela; Sarti, Paolo; Giuffre', Alessandro. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 587:14(2013), pp. 2214-2218. [10.1016/j.febslet.2013.05.047]

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

FORTE, Elena;MASTRONICOLA, Daniela;SARTI, Paolo;GIUFFRE', ALESSANDRO
2013

Abstract

Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b(558), b(595) and d. We found that the enzyme, as-prepared or in turnover with O-2, rapidly decomposes H2O2 with formation of approximately half a mole of O-2 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 (K-i similar to 2.5 mu M) and azide. The activity, possibly associated with heme-b(595), was also observed in catalase-deficient E. coli cells following cytochrome bd over-expression suggesting a protective role against oxidative stress in vivo. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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
bacteria-host interaction; hemeprotein; microbial metabolism; oxidative stress; reactive oxygen species; respiratory chain
01 Pubblicazione su rivista::01a Articolo in rivista
Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress / V. B., *borisov; Forte, Elena; Albert, Davletshin; Mastronicola, Daniela; Sarti, Paolo; Giuffre', Alessandro. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 587:14(2013), pp. 2214-2218. [10.1016/j.febslet.2013.05.047]
File allegati a questo prodotto
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/540527
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 35
  • Scopus 70
  • ???jsp.display-item.citation.isi??? 70
social impact