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10, 51-101. , and Werner, S. (1985). Eur. J. Biochem. 150, 447-454. CURRENT TOPICS IN BIOENERGETICS, VOLUME 15 Structure of the Succinate-Ubiquinone Oxidoreductase (Complex II) TOMOKO OHNISHI Department of Biochemistry Pennsylvania, Philadelphia, and Biophysics, Pennsylvania University of I. Introduction II. Iron-Sulfur Clusters of Succinate Dehydrogenase A. Identification of the Cluster Type B. Cluster Structure and Location of Iron-Sulfur Clusters Based on Amino Acid Sequence C. Spatial Organization of Redox Centers III.

Biophys. Acta 245, 240-244. , and Weiss, H. (1985). EMBO J. 4, 2075-2080. , Campbell, H. , Poulis, M. , and Young, I. G. (1981a). Biochemistry 20, 2041-2047. , Shaw, D. C , Campbell, H. , and Young, I. G. (1981b). Biochemistry 20, 3621-3628. , and Merle, P. (1981). FEBS Lett. 135, 1-11. , and Miyata, T. (1985). FEBS Lett. 189, 85-88. King, T. , and Suzuki, H. (1984). In "Biomedical and Clinical Aspects of Coenzyme Q" (K. Folkers and Y. ), Vol. 4, pp. 43-55. Elsevier, Amsterdam. Kowal, A. , Morningstar, J.

The transmembranous parts of the IP domain and, perhaps, most of the FP fragment are enclosed by a shell of hydrophobic proteins (the HP fragment), some of which are in contact with the lipid bilayer and some in contact with the aqueous phases on either side of the membrane. Electron transfer occurs from the iron-sulfur clusters of the IP fragment (clusters N-la, N-4, and others) to iron-sulfur clusters in the lipid-associated region (cluster N-2 and others), which eventually bring about reduction of ubiquinone from the pool via one or more semiquinone anion intermediates.

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