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Temperature dependence of mitochondrial oligomycin-sensitive proton transport ATPase

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Abstract

The temperature dependence of the oligomycin-sensitive ATPase (complex V) kinetic parameters has been investigated in enzyme preparations of different phospholipid composition. In submitochondrial particles, isolated complex V, and complex V reconstituted in dimirystoyl lecithin vesicles, the Arrhenius plots show discontinuities in the range 18–28°C, while no discontinuity is detected with dioleoyl lecithin recombinant. Van't Hoff plots ofK m also show breaks in the same temperature interval, with the exception of the dioleoylenzyme vesicles, whereK m is unchanged. Thermodynamic analysis of the ATPase reaction shows that DMPC-complex V has rather larger values of activation enthalpy and activation entropy below the transition temperature (24°C) than those of the other preparations, while all enzyme preparations show similar free energies of activation (14.3–18.5 kcal/mol). The results indicate that temperature and lipid composition influence to a different extent both kinetic and thermodynamic parameters of ATP hydrolysis catalyzed by the mitochondrial ATPase.

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Authors and Affiliations

  1. Istituto di Chimica Biologica, Università di Bologna, Via Irnerio 48, Italy

    G. Solaini & G. Parenti Castelli

  2. Istituto Botanico, Università di Bologna, Via Irnerio 42, Italy

    A. Baracca & G. Lenaz

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  1. G. Solaini
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  2. A. Baracca
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  3. G. Parenti Castelli
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  4. G. Lenaz
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Solaini, G., Baracca, A., Castelli, G.P. et al. Temperature dependence of mitochondrial oligomycin-sensitive proton transport ATPase. J Bioenerg Biomembr 16, 391–406 (1984). https://doi.org/10.1007/BF00743234

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  • DOI: https://doi.org/10.1007/BF00743234

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