Cytochrome bd oxidase and bacterial tolerance to oxidative and nitrosative stress.
Cytochrome bd is a prokaryotic respiratory quinol:O2 oxidoreductase, phylogenetically unrelated to the extensively studied heme-copper oxidases (HCOs). The enzyme contributes to energy conservation by generating a proton motive force, though working with a lower energetic efficiency as compared to HCOs. Relevant to patho-physiology, members of the bd-family were shown to promote virulence in some pathogenic bacteria, which makes these enzymes of interest also as potential drug targets. Beyond its role in cell bioenergetics, cytochrome bd accomplishes several additional physiological functions, being apparently implicated in the response of the bacterial cell to a number of stress conditions. Compelling experimental evidence suggests that the enzyme enhances bacterial tolerance to oxidative and nitrosative stress conditions, owing to its unusually high nitric oxide (NO) dissociation rate and a notable catalase activity; the latter has been recently documented in one of the two bd-type oxidases of Escherichia coli. Current knowledge on cytochrome bd and its reactivity with O2, NO and H2O2 is summarized in this review in the light of the hypothesis that the preferential (over HCOs) expression of cytochrome bd in pathogenic bacteria may represent a strategy to evade the host immune attack based on production of NO and reactive oxygen species (ROS). This article is part of a Special Issue entitled: 18th European Bioenergetic Conference.
CNR Institute of Molecular Biology and Pathology, Rome, Italy. Electronic address: alessandro.giuffre@uniroma1.it.
Alessandro
A
Giuffrè
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, Moscow 119991, Russian Federation.
Vitaliy B
VB
Borisov
Department of Biochemical Sciences, Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy.
Marzia
M
Arese
CNR Institute of Molecular Biology and Pathology, Rome, Italy; Department of Biochemical Sciences, Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy.
Paolo
P
Sarti
Department of Biochemical Sciences, Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University of Rome, Italy.
Elena
E
Forte
D001419:Bacteria / Q000201:enzymology / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D003580:Cytochromes / Q000378:metabolism*; D045222:Electron Transport Chain Complex Proteins / Q000378:metabolism*; D009569:Nitric Oxide / Q000378:metabolism*; D018384:Oxidative Stress; D010088:Oxidoreductases / Q000378:metabolism*
D001426:Bacterial Proteins; D003580:Cytochromes; D045222:Electron Transport Chain Complex Proteins; D009569:Nitric Oxide; D010088:Oxidoreductases
Bacterial virulence; Heme reactivity; Host-pathogen relationship; Hydrogen peroxide; Nitric oxide; Respiratory chain