On the mechanism of action of polyether XXVIII at site I of the electron-transfer chain in rat liver mitochondria

1981 ◽  
Vol 638 (1) ◽  
pp. 125-131
Author(s):  
Alfonso Carabez ◽  
Francisca Sandoval
Keyword(s):  
Electron Transfer ◽  
Rat Liver ◽  
Mechanism Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Electron Transfer Chain ◽  
Transfer Chain

Desdanine, an inhibitor of oxidative phosphorylation in mitochondria

1972 ◽  
Vol 18 (2) ◽  
pp. 265-269 ◽  
Author(s):  
Fritz Reusser
Keyword(s):  
Electron Transfer ◽  
Oxidative Phosphorylation ◽  
Respiratory Chain ◽  
Rat Liver ◽  
Mitochondrial Respiration ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Individual Reaction

The antibiotic, desdanine, acts as an uncoupling agent of oxidative phosphorylation in rat liver mitochondria. In addition, mitochondrial respiration is also impaired but to a lesser degree. Studies of individual reaction sequences occurring within the respiratory chain indicate that desdanine interferes with electron transfer at the flavoprotein regions associated with the oxidation of NADH and succinate. The flavoprotein region associated with the oxidation of succinate is more susceptible to desdanine than the NADH-linked flavoprotein region.

Phenazine Methosulfate Uptake fey Rat Liver Mitochondria

1973 ◽  
Vol 51 (3) ◽  
pp. 235-240 ◽  
Author(s):  
S. W. French ◽  
D. S. Palmer ◽  
W. A. Sim
Keyword(s):  
Electron Transfer ◽  
Molecular Oxygen ◽  
Rat Liver ◽  
Electron Flow ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Antimycin A ◽  
Phenazine Methosulfate ◽  
Temperature Dependent ◽  
Flow Through

Calcium stimulated phenazine methosulfate (PMS) accumulation by rat liver mitochondria. PMS uptake required succinate, cyanide, and low O2 tension. The NADH-generating substrate β-hydroxybutyrate did not support PMS accumulation. The rate of PMS uptake was temperature dependent. Amytal, antimycin A, oligomycin, dinitrophenol, and malonate inhibited PMS uptake indicating that electron flow through the respiratory chain was involved. A 100% O2 atmosphere caused PMS efflux from mitochondria which had accumulated PMS anaerobically. It is postulated that PMS is sequestered in mitochondria as a precipitate when reduced by electron transfer. Nonenzymatic oxidation of PMSH by molecular oxygen solubilizes it and efflux from the mitochondria follows.

scholarly journals Functional changes in rat liver mitochondria on administration of 2-methyl-4-dimethylaminoazobenzene

1984 ◽  
Vol 224 (3) ◽  
pp. 955-960 ◽  
Author(s):  
P Saikumar ◽  
C K R Kurup
Keyword(s):  
Electron Transfer ◽  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Serum Cholesterol ◽  
Oxidase Activity ◽  
Mitochondrial Fraction ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Functional Changes ◽  
Succinate Oxidase

Administration of 2-methyl-4-dimethylaminobenzene in the diet (0.1%, w/w) for 85-90 days doubled the content of mitochondria in the livers of rats. The azodye was covalently bound to liver proteins, and about 15% of the amount found in liver was associated with the mitochondrial fraction. Mitochondria isolated from the livers of azodye-fed animals showed drastically lowered ability to oxidize NAD+-linked substrates. The inhibited electron-transfer step was the reduction of ubiquinone. The organelles showed a large increase in succinate oxidase activity. The activity of cytochrome oxidase and the content of cytochrome aa3 were substantially higher in these organelles. Azodye-fed animals showed depressed serum cholesterol concentrations. The content of ubiquinone in liver also registered a small increase.

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