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Structural and Functional Features of the Eleven Constituent Proteins of the Mammalian Ubiquinol: Cytochrome c Reductase

  • Gebhard Von Jagow
  • Thomas A. Link
  • Hermann Schägger

Summary

Beef heart ubiquinol:cytochrome c reductase (the reductase) consists of 11 subunits, three catalytic and eight non-catalytic ones. The primary structures of all subunits except the two core proteins have been determined. The three catalytic subunits contain the four redox centres, i.e., three hemes and one iron-sulfur cluster, while the function of the remaining eight non-catalytic subunits has not been clearly established so far. The folding patterns derived from the amino acid sequence data indicate that all six small subunits are integral membrane proteins or anchored in the membrane. The reductase seems to be a multi-subunit complex held together predominantly by ionic bonds. The ‘core’ of the reductase is a four α-helical antiparallel bundle formed by the transmembrane helices II-V of cytochrome b, incorporating the two b-heme centres in a transmembrane arrangement.

Keywords

Small Subunit Neurospora Crassa Folding Pattern Beef Heart Amphipathic Helix 
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.

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Gebhard Von Jagow
    • 1
  • Thomas A. Link
    • 1
  • Hermann Schägger
    • 1
  1. 1.Institut für Physikalische BiochemieUniversität MünchenMunich 2West Germany

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