Abstract
Summary 1. Effective inhibition by 3-alkyl-1,4-naphthoquinones of succinate oxidation in rat-liver mitochondria requires the presence of a 2-hydroxyl group and a saturated 2′–3′ bond in the 3-alkyl side chain. 2. Basic pH renders the inhibitors less effective and their action may also be reversed by the addition of serum albumin. 3. Inorganic phosphate is required for maximum inhibition in intact mitochondria, appearing to facilitate the penetration of the inhibitor to the site of action. 4. Inhibition induced by naphthoquinones may be released to differing extents by various uncoupling agents.
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