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Cytochrome bd, a key oxidase in bacterial survival and tolerance to nitrosative stress

Academic Article
Publication Date:
2007
abstract:
Cytochrome bd is a quinol respiratory oxidase widely distributed among bacteria, where its expression favours survival under low O 2 tensions, and in the presence of nitric oxide (NO) produced by the host immune system. NO reacts with and reversibly inhibits the haem-copper terminal oxidases (HCO) where it binds at the active site, containing a haem-iron and a copper (Cu B). NO reacts also similarly with the copper lacking active site of cytochrome bd, a structural peculiarity that allows one to address the question of whether Cu B plays a role in the reaction with NO (and other ligands). In this minireview we discuss the properties of the reactions between bd-type oxidases and NO, and highlight consequences to cell/bacteria physiology.
Iris type:
01.01 Articolo in rivista
Keywords:
cytochrome; cytochrome bd terminal oxidase complex; E coli; Escherichia coli protein; multienzyme complex; nitric oxide; oxidoreductase; oxygen; adaptation; conference paper; kinetics; metabolism; microbial viability; physiology; Adaptation; Physiological; Cytochromes; Electron Transport Chain Complex Proteins; Escherichia coli Proteins; Kinetics; Microbial Viability; Nitric Oxide; Oxidoreductases; Oxygen; Bacteria (microorganisms)
List of contributors:
Brunori, Maurizio; Giuffre', Alessandro
Authors of the University:
GIUFFRE' ALESSANDRO
Handle:
https://iris.cnr.it/handle/20.500.14243/192400
Published in:
ITALIAN JOURNAL OF BIOCHEMISTRY
Journal
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http://www.scopus.com/inward/record.url?eid=2-s2.0-58249119571&partnerID=40&md5=0524aa28a7a17048779118dc969bc650
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