Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition

Borisov, Vitaliy B.; Forte, Elena; Siletsky, Sergey A.; Sarti, Paolo; Giuffrè, Alessandro

doi:10.1016/j.bbabio.2014.10.006

Cited by 40 publications

(37 citation statements)

References 70 publications

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“…Likewise, the high affinity terminal oxidase CydAB and nitrate reductase NarGH are also predicted to lack proton translocation activity. However, respiring cells can accomplish proton translocation via Q loops, when quinones are reduced on the cytoplasmic side of the cell membrane and acquire protons that are subsequently released extracellularly when quinol oxidation occurs on the opposite side of the membrane( Fig 9A )[ 40 – 42 ]. In the absence of respiration, proton extrusion via Qox or Q loops does not occur and PMF must be maintained in other ways.…”

Section: Discussionmentioning

confidence: 99%

Genetic requirements for Staphylococcus aureus nitric oxide resistance and virulence

et al. 2018

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Staphylococcus aureus exhibits many defenses against host innate immunity, including the ability to replicate in the presence of nitric oxide (NO·). S. aureus NO· resistance is a complex trait and hinges on the ability of this pathogen to metabolically adapt to the presence of NO·. Here, we employed deep sequencing of transposon junctions (Tn-Seq) in a library generated in USA300 LAC to define the complete set of genes required for S. aureus NO· resistance. We compared the list of NO·-resistance genes to the set of genes required for LAC to persist within murine skin infections (SSTIs). In total, we identified 168 genes that were essential for full NO· resistance, of which 49 were also required for S. aureus to persist within SSTIs. Many of these NO·-resistance genes were previously demonstrated to be required for growth in the presence of this immune radical. However, newly defined genes, including those encoding SodA, MntABC, RpoZ, proteins involved with Fe-S-cluster repair/homeostasis, UvrABC, thioredoxin-like proteins and the F1F0 ATPase, have not been previously reported to contribute to S. aureus NO· resistance. The most striking finding was that loss of any genes encoding components of the F1F0 ATPase resulted in mutants unable to grow in the presence of NO· or any other condition that inhibits cellular respiration. In addition, these mutants were highly attenuated in murine SSTIs. We show that in S. aureus, the F1F0 ATPase operates in the ATP-hydrolysis mode to extrude protons and contribute to proton-motive force. Loss of efficient proton extrusion in the ΔatpG mutant results in an acidified cytosol. While this acidity is tolerated by respiring cells, enzymes required for fermentation cannot operate efficiently at pH ≤ 7.0 and the ΔatpG mutant cannot thrive. Thus, S. aureus NO· resistance requires a mildly alkaline cytosol, a condition that cannot be achieved without an active F1F0 ATPase enzyme complex.

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Section: Discussionmentioning

confidence: 99%

Genetic requirements for Staphylococcus aureus nitric oxide resistance and virulence

et al. 2018

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“…Therefore, cytochrome bd typically becomes important under conditions that limit the function of these other terminal oxidases. For instance, cytochrome bd is required for respiration under low oxygen tension 2 and in the presence of nitric oxide 3 – 5 , peroxynitrite 6 , and hydrogen sulfide 7 in Escherichia coli . Moreover, E. coli cytochrome bd plays a central role in the defense against hydrogen peroxide 8 and is strongly induced upon genetic knock-out of ATP synthase 9 .…”

Section: Introductionmentioning

confidence: 99%

A fluorescence-based reporter for monitoring expression of mycobacterial cytochrome bd in response to antibacterials and during infection

Boot

Jim

Liu

et al. 2017

Sci Rep

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Cytochrome bd is a component of the oxidative phosphorylation pathway in many Gram-positive and Gram-negative bacteria. Next to its role as a terminal oxidase in the respiratory chain this enzyme plays an important role as a survival factor in the bacterial stress response. In Mycobacterium tuberculosis and related mycobacterial strains, cytochrome bd is an important component of the defense system against antibacterial drugs. In this report we describe and evaluate an mCherry-based fluorescent reporter for detection of cytochrome bd expression in Mycobacterium marinum. Cytochrome bd was induced by mycolic acid biosynthesis inhibitors such as isoniazid and most prominently by drugs targeting oxidative phosphorylation. We observed no induction by inhibitors of protein-, DNA- or RNA-synthesis. The constructed expression reporter was suitable for monitoring mycobacterial cytochrome bd expression during mouse macrophage infection and in a zebrafish embryo infection model when using Mycobacterium marinum. Interestingly, in both these infection models cytochrome bd levels were considerably higher than during in vitro culturing of M. marinum. The expression reporter described here can be a valuable tool for elucidating the role of cytochrome bd as a survival factor.

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“…The three E. coli terminal oxidases all generate a proton motive force, but cytochrome bo 3 is the only one able to pump protons, thus being twice as effective as bd -type cytochromes in terms of energy transduction 16 . Besides its role in bacterial energy metabolism, cytochrome bd -I was suggested to serve other physiological functions, being implicated in the bacterial response to oxidative and nitrosative stress 17 18 19 20 .…”

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confidence: 99%

The Terminal Oxidase Cytochrome bd Promotes Sulfide-resistant Bacterial Respiration and Growth

Forte

Borisov

Falabella

et al. 2016

Sci Rep

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Hydrogen sulfide (H2S) impairs mitochondrial respiration by potently inhibiting the heme-copper cytochrome c oxidase. Since many prokaryotes, including Escherichia (E.) coli, generate H2S and encounter high H2S levels particularly in the human gut, herein we tested whether bacteria can sustain sulfide-resistant O2-dependent respiration. E. coli has three respiratory oxidases, the cyanide-sensitive heme-copper bo3 enzyme and two bd oxidases much less sensitive to cyanide. Working on the isolated enzymes, we found that, whereas the bo3 oxidase is inhibited by sulfide with half-maximal inhibitory concentration IC50 = 1.1 ± 0.1 μM, under identical experimental conditions both bd oxidases are insensitive to sulfide up to 58 μM. In E. coli respiratory mutants, both O2-consumption and aerobic growth proved to be severely impaired by sulfide when respiration was sustained by the bo3 oxidase alone, but unaffected by ≤200 μM sulfide when either bd enzyme acted as the only terminal oxidase. Accordingly, wild-type E. coli showed sulfide-insensitive respiration and growth under conditions favouring the expression of bd oxidases. In all tested conditions, cyanide mimicked the functional effect of sulfide on bacterial respiration. We conclude that bd oxidases promote sulfide-resistant O2-consumption and growth in E. coli and possibly other bacteria. The impact of this discovery is discussed.

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Cytochrome bd from Escherichia coli catalyzes peroxynitrite decomposition

Cited by 40 publications

References 70 publications

Genetic requirements for Staphylococcus aureus nitric oxide resistance and virulence

Genetic requirements for Staphylococcus aureus nitric oxide resistance and virulence

A fluorescence-based reporter for monitoring expression of mycobacterial cytochrome bd in response to antibacterials and during infection

The Terminal Oxidase Cytochrome bd Promotes Sulfide-resistant Bacterial Respiration and Growth

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