Plant Physiol.
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Plant Physiology 69:1308-1314 (1982)
© 1982 American Society of Plant Biologists

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Articles

Interaction between Mitochondrial Cytochromes and Linoleic Acid Hydroperoxide

POSSIBLE CONFUSION WITH LIPOXYGENASE AND ALTERNATIVE PATHWAY

Jacques Dupont1, Pierre Rustin and Claude Lance

Université Pierre et Marie Curie, Laboratoire de Biologie Végétale IV, 75005 Paris, France

O2 uptake by tissue extracts in the presence of linoleic acid is generally ascribed to lipoxygenase. Such an O2 uptake can be observed not only with mitochondria of Solanum tuberosum L. and Arum maculatum L. and pure lipoxygenase but also with cytochrome c. However, the rate of oxidation is highly dependent on the procedure used to prepare the solutions of linoleic acid. Unless special care is taken to prevent contact between linoleic acid and O2, it appears that linoleic acid hydroperoxide is readily formed. This derivative can be readily oxidized by mitochondria or cytochrome c. On the other hand, the use of a rapid and specific enzymic procedure to estimate the disappearance of linoleic acid demonstrates that linoleic acid itself is not consumed at any appreciable rate by mitochondria or cytochrome c, the true substrate being linoleic acid hydroperoxide. During the reaction, the heme nucleus of added cytochrome c or of mitochondrial cytochromes undergoes deep alterations. Therefore, caution should be exerted when equating an O2 uptake observed in the presence of linoleic acid to a lipoxygenase activity. The same holds true for the similarity of reaction towards specific inhibitors between lipoxygenase and the cyanide-insensitive pathway oxidase.

1 Postal address: Laboratoire de Biologie Végétale IV, 12, Rue Curvier, 75005 Paris, France.






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