Effect of cetyltrimethylammonium on ATP hydrolysis and proton translocation in the F0-F1 H+-ATP synthase of mitochondria |
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| Authors: | Octavian Bârzu Ferruccio Guerrieri Rosanna Scarfò Giuseppe Capozza Sergio Papa |
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| Institution: | (1) Institute of Medical Biochemistry and Chemistry, University of Bari, Bari, Italy;(2) Present address: Unité de Biochimie des Regulations Cellulaires, Department de Biochimie et Genetique Moleculaire, Institut Pasteur, Paris Cedex, France |
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| Abstract: | The amphiphylic alkyl cation cetyltrimethylammonium inhibits the catalytic activity of soluble and membrane-bound F1 in a noncompetitive fashion. In sonic submitochondrial particles the Dixon plot showed a peculiar pattern with upward deviation at cetyltrimethylammonium concentration higher than 80µM. In membrane-bound F1 the inhibition by cetyltrimethylammonium was potentiated by the F0 inhibitor ologomycin. Cetyltrimethylammonium also inhibited the oligomycin-sensitive proton conductivity in F1-containing particles but was without any effect in F1-depleted particles. Also this inhibitory effect was potentiated by oligomycin. These results indicate functional cooperative interactions between F0 and F1. |
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| Keywords: | H+-ATP synthase mitochondrial F0-F1 complex ATPase H+-translocation alkyl cations |
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