http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11886
Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology (Articolo in rivista)
- Type
- Label
- Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Alternative label
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- Giuffrè A; Borisov VB; Mastronicola D; Sarti P, Forte E. (literal)
- Pagina inizio
- Pagina fine
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- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- CNR Institute of Molecular Biology and Pathology, Rome, Italy; Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russian Federation; Department of Biochemical Sciences and Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy. (literal)
- Titolo
- Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology (literal)
- 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. (literal)
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- Autore CNR
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