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