Inhibition of cytochrome oxidase activity by local anaesthetics.
Using a polarographic method, we studied the inhibition of mitochondrial electron transport at the cytochrome c oxidase site caused by eight local anaesthetics. The diversity of the types of inhibition observed indicate the importance of electrostatic interactions between the anaesthetic molecules and the membrane protein. A linear relationship was recognized between the anaesthetic activity of infiltration and the affinity for the enzyme. We also observed a significant relationship between this affinity and the octanol-water partition coefficient. This result suggests that lipophilic interactions are involved in cytochrome oxidase-anaesthetic binding. We tried to establish a parallel between this binding and the mechanism of anaesthesia involving the nerve membrane proteins.
D000779:Anesthetics, Local / Q000494:pharmacology*; D001667:Binding, Competitive; D003576:Electron Transport Complex IV / Q000037:antagonists & inhibitors*; D007700:Kinetics; D011048:Polarography; D013329:Structure-Activity Relationship
D000779:Anesthetics, Local; D003576:Electron Transport Complex IV