Adaptation of Bacillus FTU and Escherichia coli to alkaline conditions: the Na+-motive respiration

Avetisyan, A. V.; Dibrov, Pavel; Semeykina, Anna L.; Skulachev, Vladimir P.; Sokolov, Maxim

doi:10.1016/0005-2728(91)90013-e

Cited by 49 publications

(16 citation statements)

References 36 publications

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“…FTU grown under low 4iir.i+ conditions [6] were competent in Na' transport when TMPD and ascorbate were used as electron donors. The process was resistant to low concentrations of KCN [5,7,8]. The present data reveal a high degree of similarity between these oxidases.…”

Section: Introduction 2 Materials and Methodsmentioning

confidence: 53%

“…The Bat. FTU membrane particles were obtained from stationary cells by the method developed in this group [8]. The o-type oxidase was isolated and purified from membrane particles by extraction with octyl glucoside.…”

Section: Preparationsmentioning

confidence: 99%

“…Bacteria were grown in medium LB. Membrane particles were obtained as previously described [8]. The V,, of the respiratory activity of the membranes with TMPD and ascorbate was of 0.35 pmol O2 x min-' x mg-' protein.…”

Section: Preparationsmentioning

confidence: 99%

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Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

et al. 1993

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The kinetics of CO reassociation with isolated BuciZZus FTU o-type oxidase and with solubilized membranes of Escherichia coli (GO102 strain) containing the d-type oxidase only, upon laser flash photolysis under reducing conditions, were studied. In both cases, kinetics are shown to be composed of three phases (r 35-70~s 0.25-0.5 ms and 2-5 ms). The spectra of the flash-induced absorbance changes of the first kinetic components proved to be characteristic of CO-o-and CO-b,, d-cytochrome complexes in Bat. FTU and E. co/i, respectively. The spectra of the second and the third components appeared to be nearly the same in But. FTU and E. coli with peaks for the former at 436437 and 590 nm and troughs at 419-420 and 569 nm; and for the latter with peaks at 436437 and 558-560 nm and troughs at 419420 and 575-578 nm. The similarity between the putative Na'-pumping Bat. FTU o-and E. coli d-type oxidases and their difference from the H'-motive Bat. FTU cuu3-and E. coli o-type oxidases are discussed.

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Section: Introduction 2 Materials and Methodsmentioning

confidence: 53%

Section: Preparationsmentioning

confidence: 99%

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Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

et al. 1993

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“…From the physiological standpoint, this may reflect the tendency of the cells to transform the part of A~-Na* ions to A~H* also under alkaline conditions. This could be plausible especially from the kinetic and thermodynamic point of view (ApH is oriented inversely) (24). We concluded that the active Na+/H § exchanger with such feature(s) might be a clue to the adaptive bioenergetic behaviour of these cells under the different physiological conditions.…”

Section: Discussionmentioning

confidence: 77%

A study of the Na /H antiport in the archaeon Methanobacterium thermoautotrophicum strain ΔH

1997

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SummaryThe ability of the cells of Mb. thermoautotrophicum strain AH to generate a proton gradient (driven by a concentration gradient of sodium ions) at pH 6.8 as well as at pH 8 was demonstrated. The electrogenic Na+/H + antiport responsible for this process was shown to be inhibited by EIPA and also by DCCD. Artificially increasing of intracellular concentration of Ca 2+ in these cells enhanced the Na+/IT antiport activity, while the lowering of external Ca 2+ by EGTA significantly decreased this activity. The apparent K m values for Na § about 14 and 3 mM at pH 6.8 and 8, respectively, and Vm~ about 214 (pH 6.8) and 155 (pH 8) AQ/min per mg of cell proteins, respectively, were calculated. It is concluded that the described processes are mediated by the Na+/IT antiporter which might be a clue to the adaptive bioenergetic behaviour of the cells ofMb. thermoautotrophicum strain AH under the different physiological conditions.

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“…This situation is unfavorable not only from a kinetic aspect but also from a thermodynamic aspect for using H' as a coupling ion [21]. Substitution of Na' for H' as a coupling ion seems to be very effective solution to this problem.…”

Section: P Smigcin Et Al Ifebs Letters 349 (1994) 424428mentioning

confidence: 99%

Na⁺‐driven ATP synthesis in Methanobacterium thermoautotrophicum and its differentiation from H⁺‐driven ATP synthesis by rhodamine 6G

1994

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Rhodamine 6G (3 PM) effectively inhibited dpH-driven ATP synthesis in Methanobacterium thermoaurotrophicum while dpNA-driven ATP synthesis was not affected by it. Rhodamine 6G inhibited Mg"-stimulated ATPase activity of membrane vesicles prepared from these cells but the ATPase catalytic sector detached from the membrane was insensitive to this inhibitor. Methanogenesis-driven ATP synthesis at pH 6.8 of the cells grown in the presence of 50 mM NaCl was inhibited by rhodamine 6G both in the presence of 5 mM and 50 mM NaCl. On the other hand, the methanogenesis-driven ATP synthesis at pH 8.0 of cells grown in the presence of 50 mM NaCl was slightly inhibited by rhodamine 6G in the presence of 5 mM NaCl and was not inhibited at all in the presence of 50 mM NaCI. The growth experiments have shown that cells of Methanobacferium thermoautotrophicum can grow under alkaline conditions even in the presence of rhodamine 6G and of high NaCl concentration when the growth media were inoculated with the cells which had been grown in the presence of 50 mM NaCI. These results indicate that sodium-motive force-driven ATP synthase in Methanobacterium rhermoautotrophicum operates effectively at alkaline conditions and it might be the sole ATP synthesizing system when the proton motive force-supported ATP synthesis is inhibited by rhodamine 6G.

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Adaptation of Bacillus FTU and Escherichia coli to alkaline conditions: the Na+-motive respiration

Cited by 49 publications

References 36 publications

Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

A study of the Na /H antiport in the archaeon Methanobacterium thermoautotrophicum strain ΔH

Na⁺‐driven ATP synthesis in Methanobacterium thermoautotrophicum and its differentiation from H⁺‐driven ATP synthesis by rhodamine 6G

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Adaptation of Bacillus FTU and Escherichia coli to alkaline conditions: the Na+-motive respiration

Cited by 49 publications

References 36 publications

Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

Kinetics of CO binding to putative Na+‐motive oxidases of the o‐type from Bacillus FTU and of the d‐type from Escherichia coli

A study of the Na /H antiport in the archaeon Methanobacterium thermoautotrophicum strain ΔH

Na+‐driven ATP synthesis in Methanobacterium thermoautotrophicum and its differentiation from H+‐driven ATP synthesis by rhodamine 6G

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Na⁺‐driven ATP synthesis in Methanobacterium thermoautotrophicum and its differentiation from H⁺‐driven ATP synthesis by rhodamine 6G