Deficiency in ubiquinone cytochrome c reductase in a patient with mitochondrial myopathy and lactic acidosis

Proc Natl Acad Sci U S A. 1983 Aug;80(16):5103-6. doi: 10.1073/pnas.80.16.5103.


The skeletal muscle of a patient with a mitochondrial myopathy was examined. A defect in the electron transport chain was identified at the position of complex III by activity measurements and the low levels of reducible cytochrome b. The polypeptide composition of complex III in the patient's mitochondria was determined by antibody binding experiments. The method allowed detection of individual polypeptides at a lower limit of 10-40 ng of protein. Characterization of protein composition is thus possible by using a biopsy sample of 1 g of tissue. The level of core proteins, FeS protein, and subunit VI was greatly diminished in the patient's mitochondria. Cytochrome c1 polypeptide was found at normal levels but was sensitive to proteolysis by trypsin. These results show that complex III is not assembled in the patient's mitochondria. The possible role of cytochrome b as the site of the primary lesion is discussed.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acidosis / enzymology*
  • Acidosis / metabolism
  • Antigen-Antibody Complex
  • Cytochromes / metabolism
  • Electron Transport Complex III
  • Electron Transport Complex IV / metabolism
  • Humans
  • Immune Sera
  • Mitochondria, Muscle / enzymology*
  • Mitochondria, Muscle / metabolism
  • Multienzyme Complexes / deficiency*
  • Muscular Diseases / enzymology*
  • Muscular Diseases / metabolism
  • NADH, NADPH Oxidoreductases / deficiency*
  • Oxidative Phosphorylation
  • Quinone Reductases / deficiency*


  • Antigen-Antibody Complex
  • Cytochromes
  • Immune Sera
  • Multienzyme Complexes
  • NADH, NADPH Oxidoreductases
  • Quinone Reductases
  • Electron Transport Complex IV
  • Electron Transport Complex III