Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology.

Abstract : Experimental evidence suggests that the prokaryotic respiratory cytochrome bd quinol oxidase is responsible for both bioenergetic functions and bacterial adaptation to different stress conditions. The enzyme, phylogenetically unrelated to the extensively studied heme-copper terminal oxidases, is found in many commensal and pathogenic bacteria. Here, we review current knowledge on the catalytic intermediates of cytochrome bd and their reactivity towards nitric oxide (NO). Available information is discussed in the light of the hypothesis that, owing to its high NO dissociation rate, cytochrome bd confers resistance to NO-stress, thereby providing a strategy for bacterial pathogens to evade the NO-mediated host immune attack.
Document type :
Journal articles
Complete list of metadatas

Cited literature [91 references]  Display  Hide  Download

https://hal-riip.archives-ouvertes.fr/pasteur-00955432
Contributor : Istituto Pasteur Fondazione Cenci Bolognetti <>
Submitted on : Tuesday, March 4, 2014 - 2:54:13 PM
Last modification on : Wednesday, September 4, 2019 - 5:36:02 PM
Long-term archiving on: Sunday, April 9, 2017 - 8:27:35 PM

File

 Restricted access
To satisfy the distribution rights of the publisher, the document is embargoed until : jamais

Please log in to resquest access to the document

Identifiers

Collections

Citation

Alessandro Giuffrè, Vitaliy B Borisov, Daniela Mastronicola, Paolo Sarti, Elena Forte. Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology.. FEBS Letters, Wiley, 2012, 586 (5), pp.622-9. ⟨10.1016/j.febslet.2011.07.035⟩. ⟨pasteur-00955432⟩

Share

Metrics

Record views

107