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A Determination of the Molecular Weight of the Aroid Alternative Oxidase by Radiation Inactivation Analysis

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Plant Mitochondria

Abstract

Cyanide-resistant respiration occurs in a variety of plants and fungi and has been shown to be due to an “alternative” electron transfer pathway located in the mitochondrion. The alternative pathway accepts electrons from the ubiquinone pool of the main pathway and, like cytochrome oxidase in the main pathway, uses these reducing equivalents to reduce oxygen to water.1,2 The components of the alternative pathway are unknown, although it has been proposed that the pathway consists of a single complex, termed the “alternative oxidase,” which functions as a ubiquinol:oxygen oxidoreductase. In aroid spadix mitochondria, duroqulnol can be used as a water-soluble ubiquinol analogue to donate electrons to this oxidase in a cyanide-resistant, SHAM-sensitive manner. Because the detergent-solubillzed duroquinol oxidase activity has proven difficult to fractionate, we decided to investigate this enzyme using radiation inactivation analysis.

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References

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© 1987 Springer Science+Business Media New York

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Berthold, D.A., Fluke, D.J., Siedow, J.N. (1987). A Determination of the Molecular Weight of the Aroid Alternative Oxidase by Radiation Inactivation Analysis. In: Moore, A.L., Beechey, R.B. (eds) Plant Mitochondria. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-3517-5_18

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  • DOI: https://doi.org/10.1007/978-1-4899-3517-5_18

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-3519-9

  • Online ISBN: 978-1-4899-3517-5

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