Abstract
Palmitoyl-CoA is a potent inhibitor (K i = 0.15 μM) of the nicotinamide nucleotide transhydrogenase reaction catalyzed by submitochondrial particles. The inhibition is competitive selectively with NADP(H), and affects both the nonenergy-linked and energy-linked transhydrogenase reactions. A similar inhibition is demonstrated with intact mitochondria. CoA, acetyl-CoA and acetoacetyl-CoA are without effect; stearoyl-CoA acts less strongly than palmitoyl-CoA. Some implications of these results for the mechanism of the transhydrogenase reaction and its possible metabolic function are discussed.
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