Mitochondrial ATPases

Criddle, Richard S.; Johnston, Richard F.; Stack, Robert J.

doi:10.1016/b978-0-12-152509-5.50010-5

Cited by 25 publications

(5 citation statements)

References 176 publications

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“…A promising exception was a protein-bound phosphohistidine, described in Boyer's laboratory (401), which, however, turned out to be an intermediate of the succinyl thiokinase reaction (402). As could be expected, the search for chemical "high-energy" intermediates gradually decreased in intensity from the mid-1960s (although new proposals still appear occasionally [403]) .…”

Section: Search For Chemical High-energy Interme-mentioning

confidence: 79%

Mitochondria: a historical review.

Ernster¹,

Schatz²

1981

The Journal of Cell Biology

526

338

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Section: Search For Chemical High-energy Interme-mentioning

confidence: 79%

Mitochondria: a historical review.

Ernster¹,

Schatz²

1981

The Journal of Cell Biology

526

338

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“…Several properties of the granule Mg2+-dependent ATPase activity, including its inhibition by tributyltin and NN'-dicyclohexylcarbodi-imide and solubilization on extraction with dichloromethane, were similar to those of the proton-translocating ATPase of mitochondria (for reviews, see Pedersen, 1975;Criddle et al, 1979). It could be distinguished from this enzyme, however, in not being affected by oxyanions, oligomycin; azide and efrapeptin.…”

Section: Discussionmentioning

confidence: 93%

Proton-translocating Mg2+-dependent ATPase activity in insulin-secretory granules

Hutton

Peshavaria

1982

Biochemical Journal

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Insulin-secretory granules isolated from a pancreatic islet-cell tumour by centrifugation on Percoll density gradients exhibited a membrane-associated Mg(2+)-dependent ATPase activity. In granule suspensions incubated in iso-osmotic media, activity was increased 2-3-fold by carbonyl cyanide p-trifluoromethoxyphenylhydrazone, the combination of valinomycin, nigericin and K(2)SO(4) or by the addition of a detergent. Permeant anions also increased Mg(2+)-dependent ATPase activity under iso-osmotic conditions when combined with K(+) and nigericin, or NH(4) (+). It was deduced that a major component of the activity was coupled to the translocation of protons into the granule interior. The granule membrane appeared poorly permeable to H(+), K(+), NH(4) (+) and SO(4) (2-) but permeable, in increasing order, to phosphate or acetate, Cl(-), I(-) and SCN(-). Like the proton-translocating ATPase of mammalian mitochondria the granule enzyme when membrane-bound was inhibited by up to 85% by tributyltin or NN'-dicyclohexylcarbodi-imide and was solubilized in a tributyltin-insensitive form after extraction with dichloromethane. It was clearly not a mitochondrial contaminant as evidence by the distribution of marker proteins on density gradients. Unlike mitochondrial activity it was insensitive to oligomycin, efrapeptin, atractyloside, azide and oxyanions. Its properties, however, were indistinguishable from those of the proton-translocating ATPase found in the chromaffin granules of the adrenal medulla. Moreover, insulin granules and chromaffin granules exhibited similar levels of activity. This indicated that in spite of the differences in their internal composition, granules from tissues involved in polypeptide and amine hormone secretion possess catalytic components in common. Only a minor role for the ATPase in amine transport in insulin granules was apparent. Rather, its presence here may relate to the process of secretory vesicle morphogenesis or to the exocytotic mechanism.

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“…Even at the time when Mitchell's chemiosmotic theory was proposed, its acceptance was by no means universal. The leading workers in the area of bioenergetics, including stalwart scientists such as Robert J. P. Williams, David E. Green, Albert L. Lehninger, and the proponent of the first theory of oxidative phosphorylation E. C. Slater (Slater, ) were highly critical of the chemiosmotic theory and objected to it in strong terms in their last few publications on the subject (Criddle et al, ; Green, ; Pressman, ; Reynafarje et al, ; Slater, ; Williams, ). As an example, the American biochemist, pharmacologist, and discoverer of the ionophore, valinomycin concludes (Pressman, ) that, “The mechanism of biological energy transduction remains one of the most intriguing mysteries of science.…”

Section: Introductionmentioning

confidence: 99%

“…However, these laudable attempts could not be sustained over time and ultimately fizzled out. They did not have sufficiently powerful “fresh” (in the sense of (Pressman, )) unifying elements that could successfully “integrate all the available information” (in the sense of (Criddle et al, )) and were therefore unable to adequately explain the wealth of experimental data. Another reason for their “sterility” (in the words of (Green, )) could be that these attempts did not question the central aspects of chemiosmotic dogma, but rather tried to build in further refinements and achieve incremental improvements of chemiosmosis theory.…”

Section: Introductionmentioning

confidence: 99%

Oxidative phosphorylation revisited

Nath

Villadsen

2015

Biotech & Bioengineering

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The fundamentals of oxidative phosphorylation and photophosphorylation are revisited. New experimental data on the involvement of succinate and malate anions respectively in oxidative phosphorylation and photophosphorylation are presented. These new data offer a novel molecular mechanistic explanation for the energy coupling and ATP synthesis carried out in mitochondria and chloroplast thylakoids. The mechanism does not suffer from the flaws in Mitchell's chemiosmotic theory that have been pointed out in many studies since its first appearance 50 years ago, when it was hailed as a ground-breaking mechanistic explanation of what is perhaps the most important process in cellular energetics. The new findings fit very well with the predictions of Nath's torsional mechanism of energy transduction and ATP synthesis. It is argued that this mechanism, based on at least 15 years of experimental and theoretical work by Sunil Nath, constitutes a fundamentally different theory of the energy conversion process that eliminates all the inconsistencies in Mitchell's chemiosmotic theory pointed out by other authors. It is concluded that the energy-transducing complexes in oxidative phosphorylation and photosynthesis are proton-dicarboxylic acid anion cotransporters and not simply electrogenic proton translocators. These results necessitate revision of previous theories of biological energy transduction, coupling, and ATP synthesis. The novel molecular mechanism is extended to cover ATP synthesis in prokaryotes, in particular to alkaliphilic and haloalkaliphilic bacteria, essentially making it a complete theory addressing mechanistic, kinetic, and thermodynamic details. Finally, based on the new interpretation of oxidative phosphorylation, quantitative values for the P/O ratio, the amount of ATP generated per redox package of the reduced substrates, are calculated and compared with experimental values for fermentation on different substrates. It is our hope that the presentation of oxidative phosphorylation and photophosphorylation from a wholly new perspective will rekindle scientific discussion of a key process in bioenergetics and catalyze new avenues of research in a truly interdisciplinary field.

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Mitochondrial ATPases

Cited by 25 publications

References 176 publications

Mitochondria: a historical review.

Mitochondria: a historical review.

Proton-translocating Mg2+-dependent ATPase activity in insulin-secretory granules

Oxidative phosphorylation revisited

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