Energy conservation in membranes of mutants of Escherichia coli defective in oxidative phosphorylation

Nieuwenhuis, F.J.R.M.; Kanner, Baruch I.; Gutnick, David L.; Postma, Pieter W.; Dam, K. Van

doi:10.1016/0005-2728(73)90151-5

Cited by 77 publications

(39 citation statements)

References 25 publications

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“…It is of interest to note, that the transport in mutant BV4 is also completely inhibited by KCN. Although ATPase is present in this mutant [2], it cannot function to couple the hydrolysis of ATP to the generation of a high energy state, or intermediate, in agreement with cell-free studies of energy-linked transhydrogenase and ene[gy-dependent quenching of fluorescence of the dye ACMA [14,15].…”

Section: Resultssupporting

confidence: 74%

Active transport in mutants of Escherichia coli with alterations in the membrane ATPase complex

Kanner

Gutnick

1973

FEBS Letters

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Section: Resultssupporting

confidence: 74%

Active transport in mutants of Escherichia coli with alterations in the membrane ATPase complex

Kanner

Gutnick

1973

FEBS Letters

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“…Other specific oligomycins include peliomycin and botrycidin; the latter is known also as venturicidin X. Oligomycin inhibits ATP synthases from mitochondria and the chromatophores of photosynthetic bacteria (85,150,151,253,311,347,360). However, it has no or only a weak effect on photophosphorylation activity in chloroplasts and on membrane-bound ATPase activity of nonphotosynthetic bacteria (22,36,118,285,311,376). Mutagenesis studies that cause resistance to oligomycin in yeast implicate a target site residing at the interface of subunits a and c, with an involvement of both Gly23 and Glu59 of the N-and C-terminal transmembrane helices of subunit c, respectively (97,192,280).…”

Section: Polyketide Inhibitorsmentioning

confidence: 99%

ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas

Hong

Pedersen

2008

Microbiol Mol Biol Rev

275

302

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SUMMARY ATP synthase, a double-motor enzyme, plays various roles in the cell, participating not only in ATP synthesis but in ATP hydrolysis-dependent processes and in the regulation of a proton gradient across some membrane-dependent systems. Recent studies of ATP synthase as a potential molecular target for the treatment of some human diseases have displayed promising results, and this enzyme is now emerging as an attractive molecular target for the development of new therapies for a variety of diseases. Significantly, ATP synthase, because of its complex structure, is inhibited by a number of different inhibitors and provides diverse possibilities in the development of new ATP synthase-directed agents. In this review, we classify over 250 natural and synthetic inhibitors of ATP synthase reported to date and present their inhibitory sites and their known or proposed modes of action. The rich source of ATP synthase inhibitors and their known or purported sites of action presented in this review should provide valuable insights into their applications as potential scaffolds for new therapeutics for human and animal diseases as well as for the discovery of new pesticides and herbicides to help protect the world's food supply. Finally, as ATP synthase is now known to consist of two unique nanomotors involved in making ATP from ADP and Pi, the information provided in this review may greatly assist those investigators entering the emerging field of nanotechnology.

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“…When the electron transport chain is incomplete [8,9], or blocked by inhibitors or anaerobiosis, fluorescence quenching by substrate oxidation is abolished but will occur if ATP is added. The involvement of the (Ca2 +, Mg2 +)-activated ATPase in this process has been shown by the use of mutants or by treatment with ATPase inhibitors [6, has suggested that the electrochemical gradient of protons which can be formed across certain membranes of cells is of primary importance in the mechanism of biological energy conversion. The electrochemical potential difference for protons ("protonmotive force", dp) [13] in electrical units is given by the relationship dp = A$ -Z .…”

mentioning

confidence: 99%

Effect of Inhibitors on the Substrate‐Dependent Quenching of 9‐Aminoacridine Fluorescence in Inside‐Out Membrane Vesicles of Escherichia coli

Singh

Bragg

1976

European Journal of Biochemistry

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The effect of various inhibitors on the substrate-dependent quenching of the fluorescence of 9-aminoacridine was measured in inside-out membrane vesicles of Eschrriclzia coli. The rate of fluorescence quenching in the presence of inhibitors was dependent on the rate of electron transfer through the respiratory chain with NADH, succinate, D-lactate or DL-glycerol 3-phosphate as substrates. Several patterns of response were given by the inhibitors. Inhibitors competitive with substrate, or those acting only on the dehydrogenases, gave a direct relationship between the extent of inhibition of oxidase activity and the rate of quenching. A biphasic relationship was given by 2-heptyl-4-hydroxyquinoline N-oxide and piericidin A which was due to these compounds acting both as inhibitors of the respiratory chain and, at higher concentrations, as uncoupling agents. Uncouplers inhibited fluorescence quenching with minimal inhibition of oxidase activity. The transmembrane pH difference was calculated from the extent of fluorescence quenching and the intravesicular volume. The maximum pH difference of 3.3-3.7 units was generated by each of the substrates tested.The fluorescence of acridine dyes has been shown to alter with changes in the energized state of phosphorylating membranes from various sources [I -51 including Escherichia coli [6-121. In inside-out membrane vesicles of this organism the fluorescence of acridine dyes can be quenched either by substrate oxidation through the respiratory chain or by hydrolysis of ATP [6-121. When the electron transport chain is incomplete [8,9], or blocked by inhibitors or anaerobiosis, fluorescence quenching by substrate oxidation is abolished but will occur if ATP is added. The involvement of the (Ca2 +, Mg2 +)-activated ATPase in this process has been shown by the use of mutants or by treatment with ATPase inhibitors [6, has suggested that the electrochemical gradient of protons which can be formed across certain membranes of cells is of primary importance in the mechanism of biological energy conversion. The electrochemical potential difference for protons ("protonmotive force", dp) [13] in electrical units is given by the relationship dp = A$ -Z . A p H where A$ is the membrane potential, dpH is the transmembrane pH difference, and 2 is a factor to convert pH into electrical units. The energy-dependent quench- ing of the fluorescence of 9-aminoacridine was found to occur when the dye entered the internal space of chloroplasts, subchloroplast particles, chromatophores, and submitochondrial particles, in response to the transmembrane pH difference. Thus, it represents a sensitive measure of alterations in ApH with the further advantage that continuous measurements can be made [ 1,2,4,5,14].Other energy-linked functions in E. coli, including the active transport of various solutes [15], respond to the presence and absence of respiratory chain substrates and inhibitors, ATP, anaerobiosis, and mutations involving the (Ca2+, Mg'+)-activated ATPase, in a similar manner to fluorescence q...

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Energy conservation in membranes of mutants of Escherichia coli defective in oxidative phosphorylation

Cited by 77 publications

References 25 publications

Active transport in mutants of Escherichia coli with alterations in the membrane ATPase complex

Active transport in mutants of Escherichia coli with alterations in the membrane ATPase complex

ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas

Effect of Inhibitors on the Substrate‐Dependent Quenching of 9‐Aminoacridine Fluorescence in Inside‐Out Membrane Vesicles of Escherichia coli

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