Effects of Chronic Ethanol Consumption on the Respiratory Chain of Rat Liver Submitochondrial Particles

  • William S. Thayer
  • Emanuel Rubin


Studies of hepatic submitochondrial particles, which provide an experimental system allowing direct measurements of electron transfer independent of substrate transport reactions, showed that chronic ethanol ingestion (36% calories, 40 days) lowered the specific respiratory rates associated with substrate oxidation. NADH oxidase activity was decreased about 40%, succinoxidase was decreased 25%, and oxidation in ascorbate mediated by phenazine methosulfate was decreased 20%. The content of dithionite-reducible cytochrome aa 3 was decreased 38%, while that of cytochrome b was decreased 8%, and that of cytochromes c + c l was decreased 14%. Steady state kinetic measurements indicated that the turnover number of cytochrome oxidase was unchanged, about 15 s−1 under uncoupled conditions with NADH as substrate. When electron flux to cytochrome c was maximal, cytochrome c was maintained in a more highly reduced state relative to cytochrome aa 3 in submitochondrial particles from the ethanol-treated rat compared to those from the control rat. This finding is consistent with the greater decrease in cytochrome aa 3 content relative to that of cytochrome c. The results indicate that the diminished content of cytochrome oxidase is one of the factors responsible for the lower respiration rates caused by chronic ethanol consumption.


Cytochrome Oxidase Chronic Ethanol Turnover Number NADH Oxidase Phenazine Methosulfate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Bashford, C. L. and Thayer, W. S., 1977, Thermodynamics of the electrochemical proton gradient in bovine heart submitochondrial particles, J. Biol. Chem., 252:8459.Google Scholar
  2. Cederbaum, A. I., Lieber, C. S. and Rubin, E., 1974, Effects of chronic ethanol treatment on mitochondrial functions: damage to coupling site I, Arch. Biochem. Biophys., 165:560.Google Scholar
  3. Chance, B., 1952, Spectra and reaction kinetics of respiratory pigments of homogenized and intact cells, Nature 169: 215.Google Scholar
  4. DeCarli, L. M. and Lieber, C. S., 1967, Fatty liver in the rat after prolonged intake of ethanol with a nutritionally adequate new liquid diet, J. Nutr., 91:331.Google Scholar
  5. Koch, O. R., Bedetti, C. D., Gamboni, M., Montero, G. A. and Stoppani, A. O. M., 1976, Functional alterations of liver mitochondria in chronic experimental alcoholism, Exp. Molec. Pathol., 25:253.Google Scholar
  6. Lee, C. P., Ernster, L. and Chance, B., 1969, Studies of the energy transfer system of submitochondrial particles, Eur. J. Biochem.. 8:153.Google Scholar
  7. Lbw, H. and Vallin, i., 1963, Succinate-linked diphosphopyridine nucleotide reduction in submitochondrial particles, Biochim. Biophys. Acta., 69:361.Google Scholar
  8. Mustafa, M. G., Cowger, M. L., Labbe, R. F. and King, T. E., 1968, General nature of wurster’s blue shunts in the respiratory chain, J. Biol. Chem., 243:1908.Google Scholar
  9. Schnaitman, C. and Greenawalt, J. W., 1968, Enzymatic properties of the inner and outer membranes of rat liver mitochondria, J. Cell. Biol., 38:158.Google Scholar
  10. Spach, P. I., Parce, J. W. and Cunningham, C. C., 1979, Effect of chronic ethanol administration on energy metabolism and phospholipase A2 activity in rat liver, Biochem. J., 178: 23.Google Scholar
  11. Thayer, W. S. and Rubin, E., 1979, Effects of chronic ethanol intoxication on oxidative phosphorylation in rat liver submitochondrial particles, J. Biol. Chem., 254:7717.Google Scholar
  12. Thayer, W. S., Tu, Y. L. and Hinkle, P. C., 1977, Thermodynamics of oxidative phosphorylation in bovine heart submitochondrial particles, J. Biol. Chem., 252:8455.Google Scholar
  13. van Gelder, B. F., 1978, Optical properties of cytochromes from beef heart mitochondria, submitochondrial vesicles, and derived preparations, in: “Methods in Enzymology,” 53:125, S. Fleischer and L. Packer, eds., Academic Press, New York.Google Scholar

Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • William S. Thayer
    • 1
  • Emanuel Rubin
    • 1
  1. 1.Department of Pathology, Department of Biological ChemistryHahnemann Medical CollegePhiladelphiaUSA

Personalised recommendations