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  • Title: Integral polypeptide composition of Complex III of the mitochondrial electron-transfer chain.
    Author: Shimomura Y, Ozawa T.
    Journal: Biochem Int; 1984 Jan; 8(1):187-91. PubMed ID: 6089816.
    Abstract:
    Phospholipids in isolated Complex III of the mitochondrial electron-transfer chain were depleted by hydrophobic chromatography. The complex was further purified by affinity chromatography. The polypeptide composition of the complex was examined using SDS-polyacrylamide gel electrophoresis. Ten polypeptides were demonstrated in the gel pattern of the complex containing more than 10% (w/w) phospholipids; and 9 polypeptides, in the pattern of the complex containing 5% phospholipids. Although the enzymic activity of the complex composed of the 9 polypeptides was about a half of that of the original enzyme, it was fully restored when soybean phospholipid mixture was added. Further depletion of phospholipids to 0.6% makes the iron-sulfur protein dissociable from the complex, resulting in a loss of the enzymic activity (Shimomura, Y. and Ozawa, T. (1982) Biochem. Int. 5, 1-6). These results suggest that Complex III consists of 9 polypeptides, and the smallest polypeptide is a contaminant embedded in phospholipids with respect to the electron-transfer capability of the complex.
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