Negatively charged phospholipid requirement of the oligomycin-sensitive mitochondrial ATPase

Rhoderick E. Brown, Carol C. Cunningham

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11 Scopus citations


The highly-purified, oligomycin-sensitive mitochondrial adenosine triphosphatase has been reconstituted with phosphatidylserine. Treatment of the phosphatidylserine-reconstituted ATPase with phosphatidylserine decarboxylase produced a 3-fold decrease in the specific activity of the resulting phosphatidylethanolamine-enriched ATPase complex. Subsequent control experiments indicated that the resulting phosphatidylethanolamine was responsible for the lowered ATPase specific activity. These observations indicate that acidic phospholips do more than facilitate an interaction between the highly-purified, lipid-depleted ATPase and phospholipid. The negatively charged phospholipid appears to be essential for maintaining high levels of oligomycin-sensitive activity even after the initial interaction between phospholipid and the ATPase complex has occurred.

Original languageEnglish (US)
Pages (from-to)141-145
Number of pages5
JournalBBA - Biomembranes
Issue number1
StatePublished - Jan 4 1982
Externally publishedYes

Bibliographical note

Copyright 2014 Elsevier B.V., All rights reserved.


  • Mitochondrial ATPase
  • Negatively charged phospholipid
  • Phosphatidylethanolamine
  • Phosphatidylserine
  • Phosphatidylserine decarboxylase
  • Reconstitution


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