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Effect of temperature on the pathways of NADH-oxidation in broad-bean mitochondria

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Abstract

1. Respiration rates of broad-bean (Vicia faba) mitochondria were studied as a function of temperature. Arrhenius plots of all membrane-bound enzymes, as obtained with saturating substrate concentrations, revealed a break in the lower temperature range. That break was considered to indicate a phase transition of membrane phospholipids, characteristic for chilling-sensitive plants. A second discontinuity at 30°C occurred only with activities linked to energy conservation. — 2. The activation energies for the oxidation of NAD+-linked substrates differ between states 3 and 4. State 3 respiration of NAD+-linked substrates is the result a superimposition of two branches of electron transport, which can be separated by different sensibilities to rotenone. A characteristic temperature dependency of the respiratory control, as well as a shift of the low temperature break in the Arrhenius plot toward a higher temperature after state 4 to state 3 transition, are calculated to be caused by the superimposition of the two branches. — 3. The temperature dependency of the oxidation of extra-mitochondrial NADH and of succinate differs remarkably from that of the oxidation of matrix-NADH. It has been concluded that the rotenone-resistant oxidation of matrix-NADH and the oxidation of external NADH are mediated via different pathways with individual regulation sites.

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Abbreviations

BSA:

bovine serum albumin

CCCP:

carbonylcyanide-m-chlorophenylhydrazone

TPP:

thiaminepyrophosphate

References

  • Bergmeyer, H.U.: Methoden der enzymatischen Analyse. Weinheim: Chemie 1974

    Google Scholar 

  • Breidenbach, R.W., Wade, N.L., Lyons, J.M.: Effect of chilling temperatures on the activities of glyoxysomal and mitochondrial enzymes from castor bean seedlings. Plant Physiol. 54, 324–327 (1974)

    Google Scholar 

  • Crozier, W.J.: In: The kinetic basis of molecular biology, Johnson, F.H., Eyring, H., Polissar, M.J. (ed.), pp. 197–214. New York: J. Wiley and Sons 1954

    Google Scholar 

  • Day, D.A., Wiskich, J.T.: The oxidation of malate and exogenous reduced nicotinamide adenine dinucleotide-linked substrates by isolated plant mitochondria. Plant Physiol. 53, 104–109 (1974a)

    Google Scholar 

  • Day, D.A., Wiskich, J.T.: The effect of exogenous nicotinamide adenine dinucleotide on the oxidation of nicotinamide adenine dinucleotide-linked substrates by isolated plant mitochondria. Plant Physiol. 54, 360–363 (1974)

    Google Scholar 

  • Dixon, K.D., Webb, E.C.: Enzymes, 2nd ed., Chap. IV London: Longmans Green (1964)

    Google Scholar 

  • Han, M.H.: Non-linear Arrhenius plots in temperature dependent kinetic studies of enzymes reaction. J. Theor. Biol. 35, 543–568 (1972)

    Google Scholar 

  • Kumamoto, J., Raison, J.K., Lyons, J.M.: Temperature “breaks” in Arrhenius plots: A thermodynamic consequence of a phase change. J. Theor. Biol. 31, 47–51 (1970)

    Google Scholar 

  • Lee, M.P., Gear, A.R.L.: The effect of temperature on mitochondrial membrane-linked reactions. J. Biol. Chem. 249, 7541–7549 (1974)

    Google Scholar 

  • Lowry, O.H., Rosebrough, N.J., Far, A.L., Randall, R.J.: Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)

    Google Scholar 

  • Lyons, J.M., Raison, J.K.: Oxidative activity of mitochondria isolated from plant tissues sensitive and resistant to chilling injury. Plant Physiol. 45, 386–389 (1970)

    Google Scholar 

  • Lyons, J.M.: Chilling injury in plants. Ann. Rev. Plant. Physiol. 24, 445–466 (1973)

    Google Scholar 

  • Lyons, J.M., Raison, J.K., Kumamoto, J.: Polarographic determination of phase changes in mitochondrial membranes in response so temperature. In: Methods in Enzymology Vol. 32, 258–262, Colwick, S.P., Kaplak, N.O., eds. New York: Academic Press 1974

    Google Scholar 

  • Macrae, A.R.: Isolation and properties of a malic enzyme from cauliflower bud mitochondria. Biochem. J. 122, 495–501 (1971)

    Google Scholar 

  • Marx, R., Brinkmann, K.: Characteristics of rotenone-insensitive oxidation of matrix-NADH by broad bean mitochondria. Planta 142, 83–90 (1978)

    Google Scholar 

  • Massey, V., Curti, B., Ganther, H.: A temperature dependent conformational change in α-amino acid oxidase and its effects on catalysis. J. Biol. Chem. 241, 2347–2357 (1966)

    Google Scholar 

  • Miller, R.W., de la Roche, I.A., Pomeroy, M.: Structural and functional responses of wheat mitochondrial membrane to growth at low temperatures. Plant Physiol. 53, 426–433 (1974)

    Google Scholar 

  • Palm, D., Katzendobler, H.: Effect of allosteric ligands on the mechanism and stability of nicotinamide adenine dinucleotide specific isocitrate dehydrogenase from yeast. Biochemistry 11, 1283–1289 (1972)

    Google Scholar 

  • Palmer, J.M., Coleman, J.O.D.: Multiple pathways of NADH oxidation in the mitochondria. Horiz. Biochem. Biophys. 1, 220–260 (1974)

    Google Scholar 

  • Palmer, J.M., Arron, G.P.: The influence of exogenous nicotinamide adenine dinucleotide on the oxidation of malate by Jerusalem artichoke mitochondria. J. Exp. Bot. 27, 418–430 (1975)

    Google Scholar 

  • Pomeroy, M.K., Andrews, C.J.: Effect of temperature on respiration of mitochondria and shoot segments from cold-hardened and nonhardened wheat and rye seedlings. Plant Physiol. 56, 703–706 (1975)

    Google Scholar 

  • Raison, J.K., Lyons, J.M., Mehlhorn, R.J., Keith, A.D.: Temperature induced phase changes in mitochondrial membranes detected by spin labeling. J. Biol. Chem. 246, 4036–4040 (1971)

    Google Scholar 

  • Raison, J.K.: The influence of temperature-induced phase changes on the kinetics of respiratory and other membrane-associated enzyme systems. Bioenerg. 4, 559–583 (1972)

    Google Scholar 

  • Raison, J.K., Chapman, E.A., White, P.Y.: Wheat mitochondria, oxidative activity and membrane lipid structure as a function of temperature. Plant Physiol. 59, 623–627 (1977)

    Google Scholar 

  • Silvius, J.R., Read, B.D., McElhaney, R.N.: Membrane enzymes: artifacts in Arrhenius plots due to temperature dependence of substrate-binding affinity. Science 199, 902–904 (1978)

    Google Scholar 

  • Stearn, A.E.: Kinetics of biological reactions with special reference to enzymic processes. Adv. Enzym. 9, 25–27 (1949)

    Google Scholar 

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Marx, R., Brinkmann, K. Effect of temperature on the pathways of NADH-oxidation in broad-bean mitochondria. Planta 144, 359–365 (1979). https://doi.org/10.1007/BF00391579

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