Oxidative Phosphorylation and Photophosphorylation

Boyer, Paul D.; Chance, Britton; Ernster, Lars; Mitchell, Peter; Racker, Efraim; Slater, E.C.

doi:10.1146/annurev.bi.46.070177.004515

Cited by 691 publications

(185 citation statements)

References 11 publications

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“…Fl-catalyzed ATP hydrolysis (or ATP synthesis) appears either to restrict the H+-translocating activity of Fo so that only one channel at a time is operating, or to require a simultaneous H+-translocation through both channels. The latter alternative would be consistent with the need for >1 H + to be translocated for each molecule of ATP hydrolyzed or synthesized [31 ].…”

Section: Conclusion and Commentsmentioning

confidence: 74%

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H⁺‐translocation in submitochondrial particles

Kopecký¹,

Glaser²,

Norling³

et al. 1981

FEBS Letters

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Section: Conclusion and Commentsmentioning

confidence: 74%

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H⁺‐translocation in submitochondrial particles

Kopecký¹,

Glaser²,

Norling³

et al. 1981

FEBS Letters

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“…Accordingly, by using the same technique to monitor inward proton translocation in rat liver submitochondrial particles [26,32,33] ( fig.4(a)) we found complete inhibition of the energy-linked dye uptake at >1 ~g/mg oligomycin, ( fig.4(b,c)); (iv) The pH gradient existing prior to ATP addition was not affected by the platinum complexes tested ( fig.3(A,B,D)) at any concentration, thus indicating that platinum complexes do not cause ion-gradient collapse across the lysosomal membranes and, moreover, do not impair the dye's capacity to monitor pH gradients. Oligomycin also ( fig.3(B)) had no effect on the pre-existing pH gradient.…”

Section: Inhibition Of a Tp-driven Dye Uptake By Dccd And Platinum Comentioning

confidence: 99%

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

Antone

1982

FEBS Letters

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“…5 is that the sum of internal ADP and ATP increased upon energization. It remains to be seen whether the increased level of internal ATP plus ADP is simply due to the phosphorylation of internal AMP or to the freeing of tightly bound ATP and ADP by the energization of mitochondria (18).…”

Section: Phosphorylationmentioning

confidence: 99%

High-resolution 31P nuclear magnetic resonance study of rat liver mitochondria.

Ogawa¹,

Rottenberg²,

Tr³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

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Intact mitochondria were studied by highresolution 31P nuclear magnetic resonance. Observable internal phosphate compounds included inorganic phosphate (Pi), ADP, and ATP. The internal pH was determined by the chemical shift of the internal Pi, the pI( (6.7) of which was measured in uncoupled mitochondria. The observed equilibrium relation between the internal and the external Pi was consistent with the exchange equilibrium through the H2R4-/OH-carrier. RESULTS Observable phosphate compoundsA typical 31p NMR spectrum of a freshly prepared suspension of rat liver mitochondria at 00C is shown in Fig. 1A. Peaks Al and A2 are in the spectral region of phosphomonoesters, and peaks Bi and B2 are internal and external orthophosphate (Pi) resonances. Peaks Cl and C2 are in the phosphodiester region and pH insensitive. They coincide with the positions of glycerophospho(3)ethanolamine and glycerophospho(3)choline, respectively. These two peaks do not disappear after repeated washing and differential centrifugation and, therefore, most likely originate inside the mitochondria. The peak of externally added glycerophospho(3)choline coincides with peak C2, showing that the external and internal glycerophospho(3)choline are in the same magnetic environmes4 Peak D is from the terminal phosphates of ADP and/or ATP prsent inside mitochondria. The broad absorption peak E includi a phosphates of ATP and ADP, and diphosphate groups of NAt), NADP, and other diphosphodiesters. There were slight variations in relative intensities of those peaks among various' samples of similar conditions, but repeated washing did not alter the spectra appreciably. Except for peak B2 (external Pi), all peaks can be assigned to internal phosphate compounds. Fig. 1B shows the NMR spectrum of a perchloric acid extract of the mitochondrial suspension from which Fig. 1A was obtained. In this extract most of the divalent metal ions were chelated by added EDTA. The spectrum was taken at pH 8.6. The peak assignments in the extract spectrum were made by measuring the pH dependence of the chemical shifts and, most positively, by adding the likely candidates for assignment into the extract solution. The assignments in the phosphomonoester region (group a peaks) are: al, glycerol(3)phosphate; a2, not assigned; a3, AMP; a4, 2'-phosphate of NADP+ and NADPH;

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Oxidative Phosphorylation and Photophosphorylation

Cited by 691 publications

References 11 publications

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H⁺‐translocation in submitochondrial particles

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H⁺‐translocation in submitochondrial particles

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

High-resolution 31P nuclear magnetic resonance study of rat liver mitochondria.

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Oxidative Phosphorylation and Photophosphorylation

Cited by 691 publications

References 11 publications

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H+‐translocation in submitochondrial particles

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H+‐translocation in submitochondrial particles

Platinum complexes inhibit ATP‐driven basic dye uptake in lysosomes from rat liver

High-resolution 31P nuclear magnetic resonance study of rat liver mitochondria.

Contact Info

Product

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Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H⁺‐translocation in submitochondrial particles

Relationship between the binding of dicyclohexylcarbodiimide and the inhibition of H⁺‐translocation in submitochondrial particles