Protonmotive force as the source of energy for adenosine 5'-triphosphate synthesis in Escherichia coli

Wilson, Dorothy M.; Alderette, J F; Maloney, Peter C.; Wilson, Thérèse

doi:10.1128/jb.126.1.327-337.1976

Cited by 71 publications

(30 citation statements)

References 40 publications

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“…Maloney et al (14,15) recently reported ATP synthesis energized by an artificially imposed membrane potential or proton gradient in whole cells of Streptococus lactis. Similar results have been obtained using E. coli cells (5,35). Recently, an artificially imposed membrane potential (32) or proton gradient (33), in addition to oxidation, was shown to drive the synthesis of ATP in isolated membrane vesicles of E. coli.…”

Section: Time ( Sec )supporting

confidence: 76%

“…Membrane vesicles from either AN120 or AN382 failed to synthesize ATP coupled to either respiration or an artificially imposed ApH ( Table 2). Wilson et al (35) reported similar results using whole cells of AN120. It is very likely that the BFDF1 of AN382 cannot mediate proton movement, so that an electrochemical proton gradient cannot couple to ATP synthesis, nor can hydrolysis of ATP generate a protonmotive force.…”

Section: Resultsmentioning

confidence: 61%

“…The artificially imposed proton gradient and potassium gradient dissipate after a short time. If the protonmotive force becomes lower than the threshold level, supposedly about 200 mV (15,35), there would be no further detectable synthesis of ATP. Under the conditions described in this paper, acid hydrolysis of ATP might take place, since the pH of assay mixture is very low.…”

Section: Time ( Sec )mentioning

confidence: 98%

“…The effect of respiratory-chain inhibitors on ApH-driven phosphorylation demonstrates that there is no direct coupling between the respiratory chain and ATP synthesis. Likewise, Wilson et al (35) showed ATP synthesis energized by an artificial protonmotive force in intact cells of a mutant that lacks functional cytochromes. Such findings eliminate the possibility of the involvement of cytochromes in ATP synthesis.…”

Section: Time ( Sec )mentioning

confidence: 99%

“…The reversal of the sarcoplasmic reticular Ca2+ pump likewise resulted in ATP synthesis (13). In mitochondria (20), chloroplasts (9), 1 Present address: Department of Physiology, Harvard Medical School, Boston, MA 02115. and bacteria (5,15,35), a chemical gradient of proton, acid outside, has been shown to induce synthesis of ATP. Likewise, a membrane potential, which is capable of driving protons electrogenically through the F0F1, has been shown to elicit ATP formation (2,14,24).…”

mentioning

confidence: 99%

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Adenosine 5'-triphosphate synthesis driven by a protonmotive force in membrane vesicles of Escherichia coli

Tsuchiya¹

1977

J Bacteriol

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Adenosine 5'-triphosphate (ATP) synthesis energized by an artificially imposed protonmotive force (5p) in adenosine 5'-diphosphate-loaded membrane vesicles of Escherichia coli was investigated. The protonmotive force is composed of an artificially imposed pH gradient (,pH) or membrane potential (A+j), or both. A ApH was established by a rapid alteration of the pH of the assay medium. A qi\ was created by the establishment of diffusion potential of K+ in the presence of valinomycin. The maximal amount of ATP synthesized was 0.4 to 0.5 nmol/mg of membrane protein when energized by a ApH and 0.2 to 0.3 nmol/mg of membrane protein when a &P was imposed. Simultaneous imposition of both a ApH and A& resulted in the formation of greater amounts of ATP (0.8 nmol/mg of membrane protein) than with either alone. The amount of ATP synthesized was roughly proportional to the magnitude of the artificially imposed Ap. Although p-chloromercuribenzoate, 2-heptyl-4-hydroxyquinoline-Noxide, or NaCN each inhibits oxidation of 1)-lactate, and thus oxidative phosphorylation, none inhibited ATP synthesis driven by an artificially imposed Ap. Membrane vesicles prepared from uncA or uncB strains, which are defective in oxidative phosphorylation, likewise were unable to catalyze ATP synthesis when energy was supplied by an artificially imposed Ap.

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Section: Time ( Sec )supporting

confidence: 76%

Section: Resultsmentioning

confidence: 61%

Section: Time ( Sec )mentioning

confidence: 98%

Section: Time ( Sec )mentioning

confidence: 99%

mentioning

confidence: 99%

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Adenosine 5'-triphosphate synthesis driven by a protonmotive force in membrane vesicles of Escherichia coli

Tsuchiya¹

1977

J Bacteriol

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Stoichiometry of proton movements coupled to ATP synthesis driven by a pH gradient inStreptococcus lactis

Maloney

Hansen

1982

J. Membrain Biol.

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An electrochemical potential difference for H+ was established across the plasma membrane of the anaerobe Streptococcus lactis by addition of sulfuric acid to cells suspended in potassium phosphate at pH 8 along with valinomycin or permeant anions. Subsequent acidification of the cell was measured by the distribution of salicyclic acid. A comparison between cells treated or untreated with the inhibitor N,N'-dicyclohexylcarbodiimide was used to reveal that portion of net proton entry attributable to a direct coupling between H+ inflow and synthesis of ATP catalyzed by the reversible proton-translocating ATPase of this microorganism. When the imposed electrochemical proton gradient was below 180-190 mV, proton entry was at the rate expected of passive flux, for both control cells and cells treated with the ATPase inhibitor, However, at higher driving force acidification of control cells was markedly accelerated, coincident with ATP synthesis, while acidification of cells treated with the inhibitor continued at the rate characteristic of passive inflow. This observed threshold (180-190 mV) was identified as the reversal potential for this H+ "pump". Parallel measurements showed that the free energy of hydrolysis for ATP in these washed cells was 8.4 kcal/mole (370mV). The comparison between the reversal (threshold) potential and the free energy of hydrolysis for ATP indicates a stoichiometry of 2 H+/ATP for the coupling of proton movements to ATP formation in bacteria.

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A protonmotive force as the source of energy for galactoside transport in energy depletedEscherichia Coli

Flagg

Wilson

1977

J. Membrain Biol.

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An artificially produced electrochemical potential difference for protons (portonmotive force) provided the energy for the transport of galactosides in Escherichia coli cells which were depleted of their endogenous energy reserves. The driving force for the entry of protons was provided by either a transmembrane pH gradient or a membrane potential. The pH gradient across the membrane was created by acidifying the external medium. The membrane potential (inside negative) was established by the outward diffusion of potassium (in the presence of valinomycin) or by the inward diffusion of the permeant thiocyanate ion. The magnitude of the electrochemical potential difference for protons agreed well with magnitude of the chemical potential difference of the lactose analog, thiomethylgalactoside. The observations are consistent with the view that the carrier-mediated entry of each galactoside molecule is accompanied by the entry of one proton.

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Protonmotive force as the source of energy for adenosine 5'-triphosphate synthesis in Escherichia coli

Cited by 71 publications

References 40 publications

Adenosine 5'-triphosphate synthesis driven by a protonmotive force in membrane vesicles of Escherichia coli

Adenosine 5'-triphosphate synthesis driven by a protonmotive force in membrane vesicles of Escherichia coli

Stoichiometry of proton movements coupled to ATP synthesis driven by a pH gradient inStreptococcus lactis

A protonmotive force as the source of energy for galactoside transport in energy depletedEscherichia Coli

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