Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.febslet.2013.05.047 (literal)

Alternative label

• Borisov VB, Forte E, Davletshin A, Mastronicola D, Sarti P, Giuffrè A (2013)
  Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress
  in FEBS letters (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Borisov VB, Forte E, Davletshin A, Mastronicola D, Sarti P, Giuffrè A (literal)

Pagina inizio

• 2214 (literal)

Pagina fine

• 2218 (literal)

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• cited By (since 1996)0 (literal)

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• http://www.scopus.com/inward/record.url?eid=2-s2.0-84879688053&partnerID=40&md5=fab1cc963139a500ec7cd334dd3e6a8a (literal)

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• 587 (literal)

Rivista

• FEBS letters (Rivista)

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• 14 (literal)

Note

• Scopu (literal)

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• Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, Moscow 119991, Russian Federation; Department of Biochemical Sciences and Istituto Pasteur, Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy; Institute for Oriental and Classical Studies, Russian State University for the Humanities, Moscow 125993, Russian Federation; CNR Institute of Molecular Biology and Pathology, Rome, Italy (literal)

Titolo

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

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 H 2O2. 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 ~2.5 ?M) 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. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. (literal)

Prodotto di

• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)
• Institute of molecular biology and pathology (IBPM) (Istituto)

Autore CNR

• PAOLO SARTI (Persona)
• DANIELA MASTRONICOLA (Unità di personale esterno)
• ALESSANDRO GIUFFRE' (Unità di personale interno)

Insieme di parole chiave

• Parole chiave di "Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• ALESSANDRO GIUFFRE' (Unità di personale interno)
• DANIELA MASTRONICOLA (Unità di personale esterno)
• PAOLO SARTI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• FEBS letters (Rivista)

Insieme di parole chiave di

• Parole chiave di "Cytochrome bd oxidase from Escherichia coli displays high catalase activity: An additional defense against oxidative stress" (Insieme di parole chiave)