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.

scholarly journals The Swelling of Rat Liver Mitochondria by Thyroxine and its Reversal

1959 ◽  
Vol 5 (1) ◽  
pp. 97-108 ◽  
Author(s):  
Albert L. Lehninger ◽  
Betty Lou Ray ◽  
Marion Schneider
Keyword(s):  
Oxidative Phosphorylation ◽  
Temperature Coefficient ◽  
Oxidation State ◽  
Respiratory Chain ◽  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Ph Dependence ◽  
Liver Mitochondria ◽  
The Other ◽  
Rat Liver Mitochondria

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, approximately 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 KCl or NaCl but not in a 0.30 M 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.

scholarly journals Recovery of Oxidative Phosphorylation in Rat Liver Mitochondria after Whole Body Irradiation

1963 ◽  
Vol 238 (3) ◽  
pp. 1137-1140
Author(s):  
James C. Hall ◽  
Allan L. Goldstein ◽  
B.P. Sonnenblick
Keyword(s):  
Oxidative Phosphorylation ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Whole Body ◽  
Rat Liver Mitochondria

scholarly journals Inhibition by dicyclohexylcarbodiimide of proton ejection but not electron transfer in rat liver mitochondria.

1984 ◽  
Vol 259 (21) ◽  
pp. 13017-13020
Author(s):  
L Clejan ◽  
C G Bosch ◽  
D S Beattie
Keyword(s):  
Electron Transfer ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria

scholarly journals Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria

1970 ◽  
Vol 118 (1) ◽  
pp. 171-179 ◽  
Author(s):  
W. N. Aldridge ◽  
B. W. Street
Keyword(s):  
Adipose Tissue ◽  
Oxidative Phosphorylation ◽  
Brown Adipose Tissue ◽  
Binding Site ◽  
Rat Liver ◽  
Specific Binding ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Affinity Constants ◽  
Brown Adipose

1. The binding of trimethyltin and triethyltin to rat liver mitochondria was determined and the results were analysed by the method of Scatchard (1949). 2. One binding site (site 1) has the correct characteristics for the site to which trimethyltin and triethyltin are attached when they inhibit oxidative phosphorylation. For each compound the concentration of site 1 is 0.8nmol/mg of protein and the ratios of their affinity constants are the same as the ratio of the concentrations inhibiting oxidative phosphorylation. 3. Binding site 1 is present in a fraction derived from mitochondria containing only 15% of the original protein. In this preparation ultrasonication rapidly destroyed site 1. 4. Dimethyltin and diethyltin do not prevent binding of triethyltin to rat liver mitochondria, whereas triethyl-lead does. 5. Trimethyltin and triethyltin bind to mitochondria from brown adipose tissue and the results indicate a binding site 1 similar to that in rat liver mitochondria. 6. The advantages and limitations of this approach to the study of inhibitors are discussed.

scholarly journals Funiculosin; a new specific inhibitor of the respiratory chain in rat liver mitochondria

FEBS Letters ◽  
1975 ◽  
Vol 50 (2) ◽  
pp. 279-282 ◽  
Author(s):  
Ulrich K. Moser ◽  
Paul Walter
Keyword(s):  
Respiratory Chain ◽  
Rat Liver ◽  
Specific Inhibitor ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria
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