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

Alessandro Giuffrè (1) , Vitaliy B Borisov (2) , Daniela Mastronicola (1) , Paolo Sarti (1, 3) , Elena Forte (3)

1 CNR - National Research Council of Italy -
2 Belozersky Institute of Physico-Chemical Biology
3 Department of Biochemical Sciences "Rossi Fanelli"

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.

Domains: Life Sciences [q-bio]; Biochemistry, Molecular Biology

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, 2012, 586 (5), pp.622-9. ⟨10.1016/j.febslet.2011.07.035⟩. ⟨pasteur-00955432⟩