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

Rasmusson, Allan G. LU ; Møller, Ian M. and Palmer, John M. LU (1990) In FEBS Letters 259(2). p.311-314
Abstract

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... (More)

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. © 1990.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
(Arum maculatum, Plant, Mitochondria), Alternative pathway, Inside-out submitochondrial particle, Mitoplast, Trypsin
in
FEBS Letters
volume
259
issue
2
pages
4 pages
publisher
Elsevier
external identifiers
  • Scopus:0025034768
ISSN
0014-5793
DOI
10.1016/0014-5793(90)80034-G
language
English
LU publication?
yes
id
48323140-1eaf-4921-ba01-353de3ccf445
date added to LUP
2016-05-31 21:43:01
date last changed
2016-08-10 14:55:35
@misc{48323140-1eaf-4921-ba01-353de3ccf445,
  abstract     = {<p>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. © 1990.</p>},
  author       = {Rasmusson, Allan G. and Møller, Ian M. and Palmer, John M.},
  issn         = {0014-5793},
  keyword      = {(Arum maculatum, Plant, Mitochondria),Alternative pathway,Inside-out submitochondrial particle,Mitoplast,Trypsin},
  language     = {eng},
  month        = {01},
  number       = {2},
  pages        = {311--314},
  publisher    = {ARRAY(0xc0d1138)},
  series       = {FEBS Letters},
  title        = {Component of the alternative oxidase localized to the matrix surface of the inner membrane of plant mitochondria},
  url          = {http://dx.doi.org/10.1016/0014-5793(90)80034-G},
  volume       = {259},
  year         = {1990},
}