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Component of the alternative oxidase localized to the matrix surface of the inner membrane of plant mitochondria

  • Allan G. Rasmusson
  • Ian M. Møller
  • John M. Palmer
Publishing year: 1990-01-01
Language: English
Pages: 311-314
Publication/Series: FEBS Letters
Volume: 259
Issue: 2
Document type: Journal article
Publisher: Wiley-Blackwell

Abstract english

In mitoplasts from Arum maculatum spadices, succinate dehydrogenase (EC and the alternative, cyanide-resistant oxidase activity (measured as m-chlorobenzhydroxamic acid-sensitive duroquinol oxidation) was unaffected by treatment with trypsin. In contrast, when 85% inside-out submitochondrial particles were treated with trypsin the alternative oxidase activity was inhibited by about 50% and succinate dehydrogenase activity by about 40%. Thus, a trypsin-sensitive component of the alternative pathway is located on the inner surface of the inner mitochondrial membrane. After trypsin treatment of the inside-out submitochondrial particles the inhibited alternative oxidase activity was partly restored by including 0.7 M citrate in the assay medium. This indicates that trypsin does not destroy the active site but merely causes a conformational change in the enzyme, thereby lowering its activity.


  • Biochemistry and Molecular Biology
  • (Arum maculatum, Plant, Mitochondria)
  • Alternative pathway
  • Inside-out submitochondrial particle
  • Mitoplast
  • Trypsin


  • ISSN: 0014-5793
Allan Rasmusson
E-mail: allan [dot] rasmusson [at] biol [dot] lu [dot] se


Molecular Cell Biology

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