Journal of Bioenergetics and Biomembranes

, Volume 32, Issue 5, pp 507–515 | Cite as

The Oligomycin Axis of Mitochondrial ATP Synthase: OSCP and the Proton Channel

  • Rodney J. Devenish
  • Mark Prescott
  • Glen M. Boyle
  • Phillip Nagley
Article

Abstract

Oligomycin has long been known as an inhibitor of mitochondrial ATP synthase, putatively binding the Fo subunits 9 and 6 that contribute to proton channel function of the complex. As its name implies, OSCP is the oligomycin sensitivity-conferring protein necessary for the intact enzyme complex to display sensitivity to oligomycin. Recent advances concerning the structure and mechanism of mitochondrial ATP synthase have led to OSCP now being considered a component of the peripheral stator stalk rather than a central stalk component. How OSCP confers oligomycin sensitivity on the enzyme is unknown, but probably reflects important protein–protein interactions made within the assembled complex and transmitted down the stator stalk, thereby influencing proton channel function. We review here our studies directed toward establishing the stoichiometry, assembly, and function of OSCP in the context of knowledge of the organization of the stator stalk and the proton channel.

Yeast mitochondrial ATP synthase oligomycin sensitivity-conferring protein (OSCP) oligomycin Fo subunit organization proton channel stator stalk 

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Copyright information

© Plenum Publishing Corporation 2000

Authors and Affiliations

  • Rodney J. Devenish
    • 1
  • Mark Prescott
    • 1
  • Glen M. Boyle
    • 2
  • Phillip Nagley
    • 3
  1. 1.Department of Biochemistry and Molecular BiologyMonash UniversityAustralia
  2. 2.Queensland Institute of Medical ResearchHerstonAustralia
  3. 3.Department of Biochemistry and Molecular BiologyMonash UniversityAustralia

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