The Respiratory Chain of Plant Mitochondria. I. Electron Transport Between Succinate and Oxygen in Skunk Cabbage Mitochondria

The Respiratory Chain of Plant Mitochondria. I. Electron Transport Between Succinate and Oxygen... The kinetics of oxidation of ubiquinone, flavoprotein, cytochrome c , and the cytochrome b complex in skunk cabbage ( Symplocarpus foetidus ) mitochondria made anaerobic with succinate have been measured spectrophotometrically and fluorimetrically in the absence of respiratory inhibitor and in the presence of cyanide or antimycin A. No component identifiable by these means was oxidized rapidly enough in the presence of one or the other inhibitor to qualify for the role of alternate oxidase. Cycles of oxidation and rereduction of flavoprotein and ubiquinone obtained by injecting 12 μ m oxygen into the anaerobic mitochondrial suspension were kinetically indistinguishable in the presence of cyanide or antimycin A, implying that these 2 components are part of a respiratory pathway between succinate and oxygen which does not involve the cytochromes and does involve a cyanide-insensitive alternate oxidase. The cytochrome b complex shows biphasic oxidation kinetics with half times of 0.018 sec and 0.4 sec in the absence of inhibitor, which increase to 0.2 sec and 1 sec in the presence of cyanide. In the presence of antimycin A, the oxidation of the cytochrome b complex shows an induction period of 1 sec and a half-time of 3.5 sec. A split respiratory chain with 2 terminal oxidases and a branch point between the cytochromes and flavoprotein and ubiquinone is proposed for these mitochondria. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png

The Respiratory Chain of Plant Mitochondria. I. Electron Transport Between Succinate and Oxygen in Skunk Cabbage Mitochondria

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Publisher
American Society of Plant Biologist
Copyright
Copyright © 1969 by the American Society of Plant Biologists
ISSN
1532-2548
eISSN
0032-0889
DOI
10.1104/pp.44.1.115
Publisher site
See Article on Publisher Site

Abstract

The kinetics of oxidation of ubiquinone, flavoprotein, cytochrome c , and the cytochrome b complex in skunk cabbage ( Symplocarpus foetidus ) mitochondria made anaerobic with succinate have been measured spectrophotometrically and fluorimetrically in the absence of respiratory inhibitor and in the presence of cyanide or antimycin A. No component identifiable by these means was oxidized rapidly enough in the presence of one or the other inhibitor to qualify for the role of alternate oxidase. Cycles of oxidation and rereduction of flavoprotein and ubiquinone obtained by injecting 12 μ m oxygen into the anaerobic mitochondrial suspension were kinetically indistinguishable in the presence of cyanide or antimycin A, implying that these 2 components are part of a respiratory pathway between succinate and oxygen which does not involve the cytochromes and does involve a cyanide-insensitive alternate oxidase. The cytochrome b complex shows biphasic oxidation kinetics with half times of 0.018 sec and 0.4 sec in the absence of inhibitor, which increase to 0.2 sec and 1 sec in the presence of cyanide. In the presence of antimycin A, the oxidation of the cytochrome b complex shows an induction period of 1 sec and a half-time of 3.5 sec. A split respiratory chain with 2 terminal oxidases and a branch point between the cytochromes and flavoprotein and ubiquinone is proposed for these mitochondria.

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