Energization of mitochondrial inner membranes caused by l-malate |
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Authors: | Tomihiko Highti Masami Sato Syozi Mizuno Makoto Yokota Yasuo Sugiyama Yukari Nishitani Misuzu Sekiya Isamu Tani |
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Institution: | Faculty of Pharmaceutical Sciences, University of Tokushima, Shomachi, Tokushima, 770 Japan |
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Abstract: | It was found that 0.06 μg antimycin A/mg mitochondrial protein, an amount sufficient to inhibit electron transfer between cytochromes b and c1 completely, fully reversed the oxidation of cytochrome a caused by L-malate in anaerobic mitochondria. The effect of L-malate on cytochrome a was insensitive to oligomycin, but all the uncouplers and detergents tested reversed the oxidation of cytochrome a caused by L-malate in anaerobic mitochondria. It was also found that addition of L-malate to anaerobic mitochondria, like addition of ATP, decreased the fluorescence of 1-anilinonaphthalene-8-sulphonate, and that subsequent addition of uncouplers reversed this effect. The effect of L-malate on the fluorescence of the dye was insensitive to oligomycin. The present findings suggest that addition of L-malate may cause energization of the mitochondrial inner membranes and that the oxidation of cytochrome a caused by L-malate in anaerobic mitochondria may result from an L-malate-induced, energy-linked reversal of electron transfer in site II. |
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Keywords: | ANS 1-anilinonaphthalene-8-sulphonate CCCP SF 6847 |
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