The mitochondrial ATP-sensitive potassium channel (mKATP) is important in cardioprotection, although the channel remains molecularly undefined. Several studies have demonstrated that mitochondrial complex II inhibitors activate the mKATP, suggesting a potential role for complex II in channel composition or regulation. However, these inhibitors activate mKATP at concentrations which do not affect bulk complex II activity. Using the potent complex II inhibitor Atpenin A5, this relationship was investigated using tight-binding inhibitor theory, to demonstrate that only 0.4 % of total complex II molecules are necessary to activate the mKATP. These results estimate the mKATP content at 15 channels per mitochondrion.
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