Bayard T. Storey 2 a Departments of Obstetrics and Gynecology, Physiology, and Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19174 Abstract Oxidation of the respiratory chain carriers of anaerobic, CO-saturated skunk cabbage ( Symplocarpus foetidus ) mitochondria, by means of an O 2 pulse, proceeds primarily through the cyanide-insensitive alternate oxidase, since the oxidation of cytochromes a and a 3 takes place with a half-time of 3 seconds, corresponding to the rate of dissociation of CO from reduced cytochrome a 3 . Ubiquinone and part of the flavoprotein are oxidized within 1 second under these conditions, and this rapid rate of oxidation is strongly inhibited by m -chlorobenzhydroxamic acid ( m CLAM), a specific inhibitor of the alternate oxidase of plant mitochondria. The rate of ubiquinone oxidation under these conditions in white potato ( Solanum tuberosum ) mitochondria, which have no alternate oxidase, is the same as that in skunk cabbage mitochondria treated with m CLAM. Ubiquinone, thus identified as the carrier common to both the cytochrome and alternate oxidase pathways, is linked to the alternate oxidase by a flavoprotein of midpoint potential 50 millivolts more negative with which it is in equilibrium. This arrangement provides a switch for diverting electron transport primarily through the cytochrome pathway under state 3 conditions and primarily through the alternate oxidase pathway under state 4 conditions.
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