Identification of the BAL-labile factor

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Abstract
Treatment of submitochondrial particles with 2,3-dimercaptopropanol (BAL), in the presence of air, leads to the complete inactivation of the succinate oxidase system with little if any effect on the activities of succinate dehydrogenase (until more than half the BAL was oxidized) or cytochrome c oxidase. The inactivation of the complete succinate oxidase system requires the oxidation of BAL by air in the presence of the enzyme. Previous spectroscopic studies identified the block as lying between cytochromes b and c. A BAL-labile factor is present which may transfer electrons from cytochrome b to cytochrome c and which is destroyed by coupled oxidation with BAL. The present study reports that this factor is identical to the Fe-S protein in the central portion of the respiratory chain first identified by Rieske.