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Labeling of succinate cytochrome c reductase with iodine 125 accessibility of the peptides to the aqueous phases on the cytosolic and matrix sides of the mitochondrial membrane



Labeling of succinate cytochrome c reductase with iodine 125 accessibility of the peptides to the aqueous phases on the cytosolic and matrix sides of the mitochondrial membrane



Journal of Biological Chemistry 257(19): 11760-11766



Lactoperoxidase-catalyzed radioiodination was used to study the arrangement of the component peptides of [pigeon muscle] succinate-cytochrome c reductase with respect to the aqueous phases on each side of the mitochondrial inner membrane. Mitochondria depleted of their outer membrane and inside-out vesicles purified from submitochondrial particles by the lectin-affinity procedure were iodinated using immobilized preparations of lactoperoxidase. The labeled membranes were solubilized in detergent and the succinate-cytochrome c reductase was purified by immunoprecipitation with specific IgG. Analysis of the radioiodine distribution after sodium dodecyl sulfate-polyacrylamide gel electrophoresis and comparison with peptide stain patterns shows that bands 2 (64 kilodaltons), 6 (30 kilodaltons), 9 (15 kilodaltons), and 11 (< 10 kilodaltons) are labeled from the cytoplasmic surface of the membrane. Bands 1 (72 kilodaltons), 4 (48 kilodaltons), and 8 (20 kilodaltons) appear to be labeled on the matrix side of the membrane, while bands 3 (52 kilodaltons), 5 (35 kilodaltons), 7 (25 kilodaltons), and 10 (11 kilodaltons) are labeled from both sides of the membrane. Tentative identification of the labeled bands suggests that band 1 is the large subunit of succinate dehydrogenase, bands 3 and 4 represent proteins which have been referred to as core proteins I and II, bands 5 and 6 are the proteins associated with cytochromes b and c1, respectively, and band 7 is the Rieske Fe-S protein.

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