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

期刊

FEBS LETTERS
卷 586, 期 5, 页码 622-629

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.07.035

关键词

Respiratory chain; Hemeprotein; Catalytic intermediate; Nitrosative stress; Bacterial pathogen

资金

  1. Ministero dell'Istruzione, dell'Universita e della Ricerca of Italy [RBFR08F41U_001, RBIN06E9Z8, 2008FJJHKM_002]
  2. Russian Foundation for Basic Research [11-04-00031-a]

向作者/读者索取更多资源

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. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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