Stoichiometry of proton translocation coupled to substrate oxidation in plant mitochondria |
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| Authors: | Moreau F de Virville J D |
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| Affiliation: | Laboratoire de Biologie Végétale IV, Centre National de la Recherche Scientifique (UA 578), Université Pierre et Marie Curie, 12, rue Cuvier, 75005 Paris, France. |
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| Abstract: | The proton translocation coupled to the electron flux from succinate, exogenous NADH, and NAD+-linked substrates (malate and isocitrate) to cytochrome c and to oxygen was studied in purified potato (Solanum tuberosum) mitochondria using oxygen and ferricyanide pulse techniques. In the presence of valinomycin plus K+ (used as a charge compensating cation), optimum values of H+/2 e− were obtained when low amounts of electron acceptors (oxygen or ferricyanide) were added to the mitochondria (1-2 nanogram [2 e−] equivalents per milligram protein). The stoichiometry of proton translocation to electron flux was unaffected in the presence of N-ethylmaleimide, an inhibitor of the Pi/H+ symport. With succinate as substrate, H+/2 e− ratios were 4.0 ± 0.2 and 3.7 ± 0.3 with oxygen and ferricyanide as electron acceptors, respectively. With exogenous NADH, H+/2e− ratios were 4.1 ± 0.9 and 3.4 ± 0.2, respectively. The proton translocation coupled to the oxidation of NAD+-linked substrates (malate, isocitrate) was dependent upon the presence of adenylates (ADP, AMP, or ATP). For malate (+ glutamate) oxidation the observed H+/2 e− ratios were increased from 3.6 ± 2.2 to 6.5 ± 0.5 in the presence of 20 micromolar ADP. |
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