Abstract
Aurovertin inhibits oxidative phosphorylation in mitochondria in much the same way as oligomycin. Oligomycin and aurovertin, applied in amounts less than those maximally effective, have additive effects on the inhibition of oxidative phosphorylation, 32P-Pi-ATP exchange, and the exchange of 18O between Pi and water in rat liver mitochondria [1]. Aurovertin is, however, much less effective than oligomycin in inhibiting mitochondrial ATPase induced by various uncoupling agents [1, 2]. It was of great interest to find [1] that the ATPase extracted from rat liver mitochondria [3] was inhibited by aurovertin but not by oligomycin.
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