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

Alessandro Giuffrè, Vitaliy B Borisov, Daniela Mastronicola, Paolo Sarti, Elena Forte

CNR Institute of Molecular Biology and Pathology, Rome, Italy.

FEBS letters 2012 Mar 9

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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. Copyright Â© 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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. 2012 Mar 9;586(5):622-9