Abstract
The ATP-dependent K + channel (K ATP) was purified from the inner mitochondrial membrane and reconstituted into lipid bilayer membranes. K ATP activity was inhibited by high concentrations of ATP and ADP, but activated by low concentrations (up to 200 μM) of ADP. p-Diethylaminoethylbenzoate (DEB) acted as a K ATP opener: at micromolar concentrations, it reversed inhibition by ATP and ADP and it also prevented K ATP rundown. Pelargonidine, extracted from flowers of Pelargonium, reduced spontaneous activity of K ATP channels and diminished their potentiation by DEB. Their opposite action on K ATP corresponded with their opposite redox properties in reactions with free radicals: DEB behaved as an electron donor, whereas pelargonidine acted as an electron acceptor. We hypothesize that thiol groups on mitoK ATP are targets for redox-active ligans.
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