STUDIES ON THE INHIBITION OF THE MITOCHONDRIAL ATP-ase BY REDUCTION OF THE RESPIRATORY CHAIN

1960 ◽  
Vol 38 (10) ◽  
pp. 1195-1214 ◽  
Author(s):  
W. Chefurka

The effects of inhibition of the electron transport system on the stimulation of the ATP-ase reaction in liver and rat-heart mitochondria by dinitrophenol were studied. Cyanide at concentrations 10−3M and higher effectively reduced the stimulation of ATP-ase by dinitrophenol. A similar but less striking inhibition was observed for rat-heart sarcosomes. This ATP-ase reaction was also inhibited in the presence of 10−4M cyanide with glutamate, β-hydroxybutyrate, DPNH, and succinate as reductants of the respiratory chain. Anaerobiosis also caused a substantial decrease in the ATP-ase reaction. In all instances, complete inhibition of the ATP-ase reaction could not be achieved when the respiratory chain was reduced. The magnesium-stimulated ATP-ase of rat-heart sarcosomes, of aged mitochondria, and of the Keilin–Hartree heart-muscle preparation was insensitive to reduction of the carriers suggesting that this reaction may constitute only part of the total ATP-ase reaction. The compatability of the various mechanisms of oxidative phosphorylation with these results is discussed.

1960 ◽  
Vol 38 (1) ◽  
pp. 1195-1214 ◽  
Author(s):  
W. Chefurka

The effects of inhibition of the electron transport system on the stimulation of the ATP-ase reaction in liver and rat-heart mitochondria by dinitrophenol were studied. Cyanide at concentrations 10−3M and higher effectively reduced the stimulation of ATP-ase by dinitrophenol. A similar but less striking inhibition was observed for rat-heart sarcosomes. This ATP-ase reaction was also inhibited in the presence of 10−4M cyanide with glutamate, β-hydroxybutyrate, DPNH, and succinate as reductants of the respiratory chain. Anaerobiosis also caused a substantial decrease in the ATP-ase reaction. In all instances, complete inhibition of the ATP-ase reaction could not be achieved when the respiratory chain was reduced. The magnesium-stimulated ATP-ase of rat-heart sarcosomes, of aged mitochondria, and of the Keilin–Hartree heart-muscle preparation was insensitive to reduction of the carriers suggesting that this reaction may constitute only part of the total ATP-ase reaction. The compatability of the various mechanisms of oxidative phosphorylation with these results is discussed.


1984 ◽  
Vol 766 (2) ◽  
pp. 492-500 ◽  
Author(s):  
Jacques Doussiere ◽  
Erzsébet Lighti ◽  
Gérard Brandolin ◽  
Pierre V. Vignais

1996 ◽  
Vol 320 (1) ◽  
pp. 329-334 ◽  
Author(s):  
Vida MILDAZIENE ◽  
Rasa BANIENE ◽  
Zita NAUCIENE ◽  
Ausra MARCINKEVICIUTE ◽  
Ramune MORKUNIENE ◽  
...  

Stimulation of mitochondrial respiration by physiological concentrations of Ca2+ was studied to determine which components of oxidative phosphorylation are affected by Ca2+. The kinetic dependence of the respiratory chain, phosphorylation subsystem and proton leak on the mitochondrial membrane potential in isolated rat heart mitochondria respiring on 2-oxoglutarate or succinate was measured at two different concentrations of external free Ca2+. The results show that proton leak is not directly affected by Ca2+, but that both the respiratory and phosphorylation systems can be directly stimulated by Ca2+ depending on conditions. Although Ca2+ directly stimulates the phosphorylation system, this has relatively little effect on respiration rate with 2-oxoglutarate in States 3 and 4 because the subsystem has little control over respiration. However, in intermediate states, the phosphorylation system has greater control and Ca2+ stimulation of this system contributes substantially to the stimulation of respiration and phosphorylation. In the case of succinate oxidation neither the respiratory subsystem nor the phosphorylation system is stimulated by Ca2+.


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