Induction of the Escherichia Coli Cytochrome d by Low ΔH+ and by Sodium Ions

Bogachev, Alexander V.; Murtazina, Rakhilya A.; Shestopalov, Alexander I.; Skulachev, Vladimir P.

doi:10.1111/j.1432-1033.1995.tb20812.x

Cited by 25 publications

(16 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The PMF (⌬p) has been proposed as a signal being sensed by the Arc system (2,30) as ArcAB-dependent induction of cytochrome bd synthesis has been observed in aerobically growing cells by the addition of protonophores and the inducing potency of the protonophores was found to be proportional to their uncoupling activity.…”

Section: Discussionmentioning

confidence: 99%

“…Since molecular oxygen has been excluded as the biochemical signal being sensed by ArcB (24,28,38), a number of other potential signals have been proposed, including intracellular metabolites (e.g., NADH, D-lactate, and pyruvate), the redox state of the respiratory chain, and the PMF (2,22,24,30). In this study we used steady-state chemostat cultures to investigate in detail the response of E. coli to varying oxygen availability.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Effects of Limited Aeration and of the ArcAB System on Intermediary Pyruvate Catabolism in Escherichia coli

et al. 2000

View full text Add to dashboard Cite

The capacity of Escherichia coli to adapt its catabolism to prevailing redox conditions resides mainly in three catabolic branch points involving (i) pyruvate formate-lyase (PFL) and the pyruvate dehydrogenase complex (PDHc), (ii) the exclusively fermentative enzymes and those of the Krebs cycle, and (iii) the alternative terminal cytochrome bd and cytochrome bo oxidases. A quantitative analysis of the relative catabolic fluxes through these pathways is presented for steady-state glucose-limited chemostat cultures with controlled oxygen availability ranging from full aerobiosis to complete anaerobiosis. Remarkably, PFL contributed significantly to the catabolic flux under microaerobic conditions and was found to be active simultaneously with PDHc and cytochrome bd oxidase-dependent respiration. The synthesis of PFL and cytochrome bd oxidase was found to be maximal in the lower microaerobic range but not in a ⌬ArcA mutant, and we conclude that the Arc system is more active with respect to regulation of these two positively regulated operons during microaerobiosis than during anaerobiosis.Escherichia coli possesses distinct catabolic routes that enable it to conserve energy efficiently under wide ranges of redox conditions. In environments that provide the cell with external electron acceptors such as oxygen, nitrate, fumarate, and dimethyl sulfoxide, reoxidation of reducing equivalents generated by the oxidation of the energy source occurs in the respiratory chain. This process can be coupled to the formation of a proton motive force (PMF) and thus constitutes an efficient pathway for energy conservation. In the absence of oxygen or other external electron acceptors, ATP synthesis occurs at the level of substrate phosphorylation. Under such fermentative conditions E. coli, when growing on glucose, excretes specific products such as ethanol, acetate, lactate, succinate, and formate (or CO 2 and H 2 ). The relative rates of formation of these products are governed by the demand for redox neutrality (5, 21).The actual in vivo fluxes of carbon and electrons through the various pathways are determined largely by three major branch points (Fig. 1). The first of these involves the cleavage of pyruvate, which serves as a common substrate for pyruvate formate-lyase (PFL) and the pyruvate dehydrogenase complex (PDHc). Entry into the fermentative pathway depends largely on the activity of PFL, whereas entry into the respiratory pathway is largely governed by the activity of the PDHc. At the second branch point, acetyl-coenzyme A, the product of both of the above reactions, can be converted to either the major fermentation products acetate and ethanol or can subsequently undergo further oxidation in the tricarboxylic acid (TCA) cycle. Finally, E. coli also possesses a branched respiratory chain. The electron flow into respiration can follow alternative routes to oxygen, via a coupled or an uncoupled NADH dehydrogenase (NDH-1 or NDH-2, respectively) to quinone (19,42). Quinol is then oxidized by either the cytochrome bd or th...

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Effects of Limited Aeration and of the ArcAB System on Intermediary Pyruvate Catabolism in Escherichia coli

et al. 2000

View full text Add to dashboard Cite

show abstract

“…There have been reports that the cytochrome d terminal oxidase of E. coli is not an H ϩ pump (162) but a Na ϩ pump (6,8,15,135). An Na ϩ -transporting terminal oxidase has also been found in a representative of the genus Bacillus (8,115,178), later identified as Bacillus halodurans (71) (Table 1) but, rather, tentatively consider them to be H ϩ pumps (Table 2).…”

Section: ؉ -Transporting Terminal Oxidasesmentioning

confidence: 99%

Sodium Ion Cycle in Bacterial Pathogens: Evidence from Cross-Genome Comparisons

Häse

Fedorova

Galperin

et al. 2001

Microbiol Mol Biol Rev

218

166

View full text Add to dashboard Cite

Analysis of the bacterial genome sequences shows that many human and animal pathogens encode primary membrane Na+ pumps, Na+-transporting dicarboxylate decarboxylases or Na+-translocating NADH:ubiquinone oxidoreductase, and a number of Na+-dependent permeases. This indicates that these bacteria can utilize Na+ as a coupling ion instead of or in addition to the H+ cycle. This capability to use a Na+ cycle might be an important virulence factor for such pathogens as Vibrio cholerae, Neisseria meningitidis, Salmonella enterica serovar Typhi, and Yersinia pestis. In Treponema pallidum, Chlamydia trachomatis, and Chlamydia pneumoniae, the Na+ gradient may well be the only energy source for secondary transport. A survey of preliminary genome sequences of Porphyromonas gingivalis, Actinobacillus actinomycetemcomitans, and Treponema denticola indicates that these oral pathogens also rely on the Na+ cycle for at least part of their energy metabolism. The possible roles of the Na+ cycling in the energy metabolism and pathogenicity of these organisms are reviewed. The recent discovery of an effective natural antibiotic, korormicin, targeted against the Na+-translocating NADH:ubiquinone oxidoreductase, suggests a potential use of Na+ pumps as drug targets and/or vaccine candidates. The antimicrobial potential of other inhibitors of the Na+ cycle, such as monensin, Li+ and Ag+ ions, and amiloride derivatives, is discussed

show abstract

“…Nevertheless, these oxidases clearly differ in induction conditions. The A. vinelandii bd-type oxidase is induced by an [02] increase whereas the E. coli enzyme is induced under conditions when protonic potential decreases [14], in particular by lowering the 02 concentration [15]. This is why Poole has suggested that the bd-type oxidases of ,4. vinelandii and E. coli perform different functions [8].…”

Section: Introductionmentioning

confidence: 99%

Generation of protonic potential by the bd‐type quinol oxidase of Azotobacter vinelandii

1997

View full text Add to dashboard Cite

Inside-out subcellular vesicles of Azotobacter vinelandii are found to produce ApH and A~P (interior acidic and positive) when oxidising malate or menadiol. These effects are inherent in both Cyd+Cyo -(lacking the o-type oxidase) and Cyd Cyo + (lacking the bd-type oxidase) strains. They appear to be myxothiazol-sensitive in the Cyd-Cyo + strain but not in the Cyd+Cyo -strain. The H+/e -ratio for the terminal part of respiratory chain of a bd-type oxidase overproducing strain is established as being close to I. It is also shown that NADH oxidation by the vesicles from the Cyd-Cyo + strain is sensitive to low concentrations of myxothiazol and antimycin A whereas that of the Cyd+Cyo -strain is resistant to these Q-cycle inhibitors. It is concluded that (i) the bd-type oxidase of A. vinelandii is competent in generating a protonic potential but its efficiency is lower than that of the o-type oxidase and (ii) Q-cycle does operate in the o-type cytochrome oxidase terminated branch of the A. vinelandii respiratory chain and does not in the bd-type quinol oxidase terminated branch. These relationships are discussed in the context of the respiratory protection function of the bd-type oxidase in A. vinelandii.

show abstract

Induction of the Escherichia Coli Cytochrome d by Low Δ_H+ and by Sodium Ions

Cited by 25 publications

References 49 publications

Effects of Limited Aeration and of the ArcAB System on Intermediary Pyruvate Catabolism in Escherichia coli

Effects of Limited Aeration and of the ArcAB System on Intermediary Pyruvate Catabolism in Escherichia coli

Sodium Ion Cycle in Bacterial Pathogens: Evidence from Cross-Genome Comparisons

Generation of protonic potential by the bd‐type quinol oxidase of Azotobacter vinelandii

Contact Info

Product

Resources

About