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

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Author

Summary, in English

In mitoplasts from Arum maculatum spadices, succinate dehydrogenase (EC 1.3.99.1) 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.

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

Topic

  • Biochemistry and Molecular Biology

Keywords

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

Status

Published

Research group

  • Plant Biology

ISBN/ISSN/Other

  • ISSN: 0014-5793