Effect of pesticides “Butylcaptax (Russia)” and “Droppa (Russia)” on respiration and oxidative phosphorylation of liver mitochondria of pregnant rats and their embryos

The article provides information on the effect of pesticides - butylcaptax and droppa on respiration and oxidative phosphorylation of liver mitochondria in rat rats and their embryos. It has been shown that butylcaptax and droppa reduce the oxidation of succinate and α-ketoglutarate in the V4*, V3 and Vdnf states and drug conjugation in the liver mitochondria of pregnant animals and their embryos. The most significant inhibition of ADF formation in the respiratory chain of fatal and maternal liver mitochondria occurs via the NAD-dependent pathway, especially when poisoning with butylcaptax on the 19th day of pregnancy. Apparently, inhibition of ADF-stimulated respiration is associated with inhibition of electron transfer along the respiratory chain or is a consequence of inhibition of the transport of phosphate or ADF into mitochondria, which plays a key role in the mechanism of oxidative phosphorylation. A decrease in the conjugation of oxidation and phosphorylation does not create conditions for the accumulation of energy in an utilizable form - in the form of ADF.

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Desdanine, an inhibitor of oxidative phosphorylation in mitochondria

Canadian Journal of Microbiology ◽

10.1139/m72-040 ◽

1972 ◽

Vol 18 (2) ◽

pp. 265-269 ◽

Cited By ~ 1

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.

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The Swelling of Rat Liver Mitochondria by Thyroxine and its Reversal

The Journal of Cell Biology ◽

10.1083/jcb.5.1.97 ◽

1959 ◽

Vol 5 (1) ◽

pp. 97-108 ◽

Cited By ~ 110

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.

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Sensitivity to NN'-dicyclohexylcarbodi-imide of proton translocation by mitochondrial NADH:ubiquinone oxidoreductase

Biochemical Journal ◽

10.1042/bj2370927 ◽

1986 ◽

Vol 237 (3) ◽

pp. 927-930 ◽

Cited By ~ 12

Author(s):

P J Honkakoski ◽

I E Hassinen

Keyword(s):

Electron Transfer ◽

Respiratory Chain ◽

Proton Translocation ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Nadh:Ubiquinone Oxidoreductase ◽

Proton Extrusion ◽

Ferricyanide Reduction ◽

Isolated Rat Liver ◽

Isolated Rat

Proton extrusion during ferricyanide reduction by NADH-generating substrates or succinate was studied in isolated rat liver mitochondria with the use of optical indicators. NN'-Dicyclohexylcarbodi-imide (DCCD) caused a decrease of 84% in the H+/e- ratio of NADH:cytochrome c reduction, but a decrease of only 49% in that of succinate:cytochrome c reduction, even though electron transfer was decreased equally in both spans. The data indicate that a DCCD-sensitive channel operates in the NADH:ubiquinone oxidoreductase region of the respiratory chain.

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Arsenate Uncoupling of Oxidative Phosphorylation in Isolated Plant Mitochondria

Functional Plant Biology ◽

10.1071/pp9760153 ◽

1976 ◽

Vol 3 (2) ◽

pp. 153 ◽

Cited By ~ 3

Author(s):

W.A Wickes ◽

J.T Wiskish

Keyword(s):

Electron Transfer ◽

Oxidative Phosphorylation ◽

Plant Mitochondria ◽

Liver Mitochondria ◽

Rat Liver Mitochondria ◽

Transfer Processes ◽

Uncoupling Of Oxidative Phosphorylation ◽

Electron Transfer Processes ◽

Stimulation Of ◽

Malate Oxidation

The uncoupling by arsenate of beetroot and cauliflower bud mitochondria showed the following characteristics: (1) arsenate stimulation of respiration above the rate found with phosphate; (2) inhibition of arsenate-stimulated respiration by phosphate; (3) enhancement of arsenate-stimulated respiration by ADP; (4) only partial prevention of this ADP-enhanced respiration by atractyloside; (5) inhibition by oligomycin of the arsenate-stimulated respiration back to the phosphate rate; and (6) the absence of any stimulatory effect of ADP in the presence of oligomycin. These results are qualitatively analogous to those reported for arsenate uncoupling in rat liver mitochondria. Arsenate stimulated malate oxidation, presumably by stimulating malate entry, in both beetroot and cauliflower bud mitochondria; however, high rates of oxidation, and presumably entry, were only sustained with arsenate in beetroot mitochondria. NADH was oxidized rapidly in cauliflower bud mitochondria in the presence of arsenate, showing that arsenate did not inhibit electron transfer processes.

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