Oxidative Phosphorylation

Lehninger, Albert L.; Wadkins, Charles L.; Gamble, James L.; Cooper, Cecil; Devlin, Thomas M.

doi:10.1126/science.128.3322.450

Cited by 147 publications

(26 citation statements)

References 21 publications

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“…Discussion. The "recombination" of the DNP-insensitive soluble ATP-ADP exchange enzyme with phosphorylating digitonin particles to reconfer DNPsensitivity is fully consistent with and provides further support for a general mechanism of respiratory energy coupling postulated earlier: [2][3][4][5] (1) Carrier --X + P1 i P X + Carrier (2) P-X+± E ±P--E+X (3) P -E + ADP T ATP + E where Carrier '-X is the chemical species of the electron carrier in which is conserved oxido-reduction energy, and X and E are group-transferring enzymes. E is the enzyme catalyzing the ATP-ADP exchange reaction, which has another active site reactive with P -X.…”

supporting

confidence: 82%

Reconstitution of the Dinitrophenol-Sensitive Atp-Adp Exchange Reaction of Oxidative Phosphorylation

Wadkins¹,

Lehninger²

1960

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

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Intact rat liver mitochondrial as well as fragments of mitochondrial membranes capable of oxidative phosphorylation2 catalyze an exchange reaction between ATP and ADP which is inhibited by 2,4-dinitrophenol (DNP). The exchange enzyme has been postulated to catalyze the terminal reaction of oxidative phosphorylation by which ATP is formed.'-5 The ATP-ADP exchange reaction is inhibited by dinitrophenol only in freshly prepared particles capable of phosphorylation; aging of the particles causes no loss of activity of the exchange but results in loss of its DNP-sensitivity.2 Similarly, azide has no inhibitory effect on the ATP-ADP exchange, but abolishes its sensitivity to DNP.2 The stability of the ATP-ADP exchange enzyme made possible its extraction in soluble form2 and its purification to a high degree.6 The soluble form of the enzyme is completely insensitive to DNP.2,6These findings thus show that DNP-sensitivity is not intrinsic but is conferred on the ATP-ADP exchange in fresh mitochondria or membrane fragments because it is in functional equilibrium with an earlier enzymatic reaction of the respiratory energy coupling mechanism which is sensitive to DNP, from which it can be dissociated by aging, azide, or physical separation. This paper describes the restoration of DNP-sensitivity to the soluble, DNPinsensitive ATP-ADP exchange enzyme separated from rat liver mitochondria, by recombining it with mitochondrial membrane fragments prepared by the action of digitonin.7 Such "recombination," which is specific, indicates that the soluble ATP-ADP exchange enzyme we have isolated is a participant in the mechanism of respiratory energy-coupling and differentiates it from other mitochondrial enzymes catalyzing ATP-ADP exchanges2 which are not relevant to oxidative phosphorylation.Methods.-The ATP-ADP exchange rate was measured with p32-or C'4-labeled ADP using the paper chromatographic separation described before.2 Initial incorporation rates under conditions of substrate saturation were measured. Phosphorylating digitonin particles from rat liver mitochondria were prepared according to Devlin and Lehninger.7 Soluble ATP-ADP exchange enzyme was prepared according to Wadkins and Lehninger.2 The purification of the ATP-ADP ex-

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supporting

confidence: 82%

Reconstitution of the Dinitrophenol-Sensitive Atp-Adp Exchange Reaction of Oxidative Phosphorylation

Wadkins¹,

Lehninger²

1960

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

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“…It has been suggested (Ogston and Smithies, 1948;Chance and Williams, 1956;Lehninger et al, 1958) that the electron transfer carrier protein molecules are intimately organized into replicated units or FIGURE 11 A portion of the field shown in Fig. 10, at higher magnification.…”

Section: Discussionmentioning

confidence: 99%

THE STRUCTURE OF FLIGHT MUSCLE SARCOSOMES IN THE BLOWFLY CALLIPHORA ERYTHROCEPHALA (DIPTERA)

Smith

1963

The Journal of Cell Biology

151

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The electron microscopic structure of sectioned indirect flight muscle fibers of the blowfly Callipkora is described. Particular attention is paid to the organization of the sarcosomes (mitochondria) of this tissue, and this description is accompanied by an account of the appearance of these bodies in negatively stained preparations. In sectioned material, it has been shown that these sarcosomes are similar to other mitochondria in the disposition of the outer and inner limiting membranes, but that the cristae, confluent with the latter, are unusually regular, and form parallel plates, containing circular fenestrations forming cylindrical channels within the matrix. Negatively stained preparations of disrupted sarcosomes reveal that both the outer limiting membrane and the cristae membranes bear large numbers of small particles, similar in appearance to those described by FernfindezMoran and others in various mitochondria. In Calliphora, these particles consist of a subspherical "head" and a cylindrical "stalk," and appear to be arranged on the mitochondrial membranes either randomly distributed, or collected into circular or elongated groups. Recent suggestions concerning the nature of these submitochondrial particles are discussed, and an attempt is made to correlate the aspects of organization of Calliphora sarcosomes, revealed by conventional sectioning of the "intact" structures, and by negative staining of sarcosomal derivatives.

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“…references 6,42). A bound form of DPN reactive in phosphorylating respiration with D-/3-hydroxybutyric dehydrogenase appears to be present in phosphorylating submitochondrial fragments (51).…”

Section: Existence Of Different Types and Stages Of Milochondrial Swementioning

confidence: 99%

The Swelling of Rat Liver Mitochondria by Thyroxine and its Reversal

Lehninger¹,

Ray²,

Schneider³

1959

The Journal of Cell Biology

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143

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The in vitro swelling action of L-thyroxine on rat liver mitochondria as examined photometrically represents an acceleration of a process which the mitochondria are already inherently capable of undergoing spontaneously, as indicated by the identical kinetic characteristics and the extent of thyroxine-induced and spontaneous swelling, the nearly identical pH dependence, and the fact that sucrose has a specific inhibitory action on both types of swelling. However, thyroxine does not appear to be a "catalyst" or coenzyme since it does not decrease the temperature coefficient of spontaneous swelling. The temperature coefficient is very high, approximatNy 6.0 near 20 °.Aging of mitochondria at 0 ° causes loss of thyroxine sensitivity which correlates closely with the loss of bound DPN from the mitochondria, but not with loss of activity of the respiratory chain or with the efficiency of oxidative phosphorylation. Tests with various respiratory chain inhibitors showed that the oxidation state of bound DPN may be a major determinant of thyroxine sensitivity; the oxidation state of the other respiratory carriers does not appear to influence sensitivity to thyroxine. These facts and other considerations suggest that a bound form of mitochondrial DPN is the "target" of the action of thyroxine.The thyroxine-induced swelling is not reversed by increasing the osmolar concentration of external sucrose, but can be "passively" or osmotically reversed by adding the high-particle weight solute polyvinylpyrrolidone. The mitochondrial membrane becomes more permeable to sucrose during the swelling reaction. On the other hand, thyroxine-induced swelling can be "actively" reversed by ATP in a medium of 0.15 M KC1 or NaC1 but not in a 0.30 ~ sucrose medium. The action of ATP is specific; ADP, Mn +*, and ethylenediaminetetraacetate are not active. It is concluded that sucrose is an inhibitor of the enzymatic relationship between oxidative phosphorylation and the contractility and permeability properties of the mitochondrial membrane.Occurrence of different types of mitochondrial swelling, the intracellular factors affecting the swelling and shrinking of mitochondria, as well as the physiological significance of thyroxine-induced swelling are discussed.

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Oxidative Phosphorylation

Cited by 147 publications

References 21 publications

Reconstitution of the Dinitrophenol-Sensitive Atp-Adp Exchange Reaction of Oxidative Phosphorylation

Reconstitution of the Dinitrophenol-Sensitive Atp-Adp Exchange Reaction of Oxidative Phosphorylation

THE STRUCTURE OF FLIGHT MUSCLE SARCOSOMES IN THE BLOWFLY CALLIPHORA ERYTHROCEPHALA (DIPTERA)

The Swelling of Rat Liver Mitochondria by Thyroxine and its Reversal

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