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Volumn 136, Issue 2, 1998, Pages 149-157

Coordinate control by Mg2+ of the phosphorylative activities and of the succinate dehydrogenase of higher plant mitochondria

Author keywords

Adenine nucleotides; Magnesium; Phosphorylative activity; Plant mitochondria; Pyrophosphate; Succinate dehydrogenase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CALCIUM; CITRIC ACID; EDETIC ACID; INORGANIC PYROPHOSPHATASE; MAGNESIUM; PROTON; SUCCINATE DEHYDROGENASE;

EID: 0032483306     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(98)00114-9     Document Type: Article
Times cited : (5)

References (39)
  • 1
    • 0011870367 scopus 로고
    • Are biosynthetic reactions in plant cells thermodynamically coupled to glycolysis and the tonoplast proton motive force?
    • Taiz L. Are biosynthetic reactions in plant cells thermodynamically coupled to glycolysis and the tonoplast proton motive force? J. Theor. Biol. 123:1986;231-238.
    • (1986) J. Theor. Biol. , vol.123 , pp. 231-238
    • Taiz, L.1
  • 2
    • 0001343924 scopus 로고
    • Fructose-2,6-bisphosphate as a regulatory molecule in plants
    • Stitt M. Fructose-2,6-bisphosphate as a regulatory molecule in plants. Ann. Rev. Plant Physiol. Mol. Biol. 41:1990;153-158.
    • (1990) Ann. Rev. Plant Physiol. Mol. Biol. , vol.41 , pp. 153-158
    • Stitt, M.1
  • 7
    • 0008904464 scopus 로고
    • Oxidation-linked formation of inorganic pyrophosphate in maize shoot mitochondria
    • Kowalczyk S., Maslowski P. Oxidation-linked formation of inorganic pyrophosphate in maize shoot mitochondria. Biochim. Biophys. Acta. 766:1984;570-575.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 570-575
    • Kowalczyk, S.1    Maslowski, P.2
  • 9
    • 0019879466 scopus 로고
    • A comparison of the phosphorylation potential and electrochemical proton gradient in mung bean mitochondria and phosphorylating sub-mitochondrial particles
    • Moore A.L., Bonner W.D. Jr. A comparison of the phosphorylation potential and electrochemical proton gradient in mung bean mitochondria and phosphorylating sub-mitochondrial particles. Biochim. Biophys. Acta. 634:1981;117-128.
    • (1981) Biochim. Biophys. Acta , vol.634 , pp. 117-128
    • Moore, A.L.1    Bonner W.D., Jr.2
  • 10
    • 0002819542 scopus 로고    scopus 로고
    • Characterization of adenylate kinase in intact mitochondria of fertile and male sterile potato (Solanum tuberosum L.)
    • Busch K., Ninnemann H. Characterization of adenylate kinase in intact mitochondria of fertile and male sterile potato (Solanum tuberosum L.). Plant Sci. 116:1996;1-8.
    • (1996) Plant Sci. , vol.116 , pp. 1-8
    • Busch, K.1    Ninnemann, H.2
  • 11
    • 0001661817 scopus 로고
    • Equilibration of adenylates by maize leaf adenylate kinase: Effect of magnesium on apparent true equilibria
    • Kleczkowski L.A.M., Randall D.D. Equilibration of adenylates by maize leaf adenylate kinase: effect of magnesium on apparent true equilibria. J. Exp. Bot. 42:1991;537-540.
    • (1991) J. Exp. Bot. , vol.42 , pp. 537-540
    • Kleczkowski, L.A.M.1    Randall, D.D.2
  • 12
    • 0343467115 scopus 로고
    • Intramitochondrial location of adenylate kinase
    • Arron G.P., Day D.A., Laties G.G. Intramitochondrial location of adenylate kinase. Plant Physiol. 61S:1978;84.
    • (1978) Plant Physiol. , vol.61 , pp. 84
    • Arron, G.P.1    Day, D.A.2    Laties, G.G.3
  • 15
  • 16
    • 0343467116 scopus 로고
    • Regulation, of oxidative phosphorylation in plant mitochondria
    • C.S. Levings III, & I.K. Vasil. Dordrecht: Kluwer
    • Whitehouse D.G., Moore A.L. Regulation, of oxidative phosphorylation in plant mitochondria. Levings III C.S., Vasil I.K. The Molecular Biology of Plant Mitochondria. 1995;313-344 Kluwer, Dordrecht.
    • (1995) The Molecular Biology of Plant Mitochondria , pp. 313-344
    • Whitehouse, D.G.1    Moore, A.L.2
  • 17
    • 0026562169 scopus 로고
    • The role(s) of adenylate kinase and the adenylate carrier in the regulation of plant mitochondrial respiratory activity
    • Fricaud A.C., Walters A.J., Whitehouse D.G., Moore A.L. The role(s) of adenylate kinase and the adenylate carrier in the regulation of plant mitochondrial respiratory activity. Biochim. Biophys. Acta. 1099:1992;253-261.
    • (1992) Biochim. Biophys. Acta , vol.1099 , pp. 253-261
    • Fricaud, A.C.1    Walters, A.J.2    Whitehouse, D.G.3    Moore, A.L.4
  • 18
    • 0030816994 scopus 로고    scopus 로고
    • The controlling influence of ADP, ATP and magnesium on the activities of adenylate kinase, ATP synthase, ADP/ATP translocator and the mitochondrial respiration in plants
    • Busch K., Ninnemann H. The controlling influence of ADP, ATP and magnesium on the activities of adenylate kinase, ATP synthase, ADP/ATP translocator and the mitochondrial respiration in plants. Plant Sci. 128:1997;85-95.
    • (1997) Plant Sci. , vol.128 , pp. 85-95
    • Busch, K.1    Ninnemann, H.2
  • 19
    • 0000163072 scopus 로고
    • The tricarboxylic acid cycle in plant mitochondria: Its operation and regulation
    • in: A. Pirson, M.H. Zimmermann (Eds.), Springer-Verlag, New York
    • J.T. Wiskich, I.B. Dry, The tricarboxylic acid cycle in plant mitochondria: its operation and regulation, in: A. Pirson, M.H. Zimmermann (Eds.), Encyclopedia of Plant Physiology, New Series, vol. 18, Springer-Verlag, New York, 1985, pp. 281-313.
    • (1985) Encyclopedia of Plant Physiology, New Series , vol.18 , pp. 281-313
    • Wiskich, J.T.1    Dry, I.B.2
  • 20
    • 0000653060 scopus 로고
    • Regulation of succinate dehydrogenase in higher plants. II. Activation by substrates, reduced coenzyme Q, nucleotides, and anions
    • Oestreicher G., Hogue P., Singer T.P. Regulation of succinate dehydrogenase in higher plants. II. Activation by substrates, reduced coenzyme Q, nucleotides, and anions. Plant Physiol. 52:1973;622-626.
    • (1973) Plant Physiol. , vol.52 , pp. 622-626
    • Oestreicher, G.1    Hogue, P.2    Singer, T.P.3
  • 21
    • 0000653060 scopus 로고
    • Regulation of succinate dehydrogenase in higher plants. I. Some general characteristics of the membrane-bound enzyme
    • Singer T.P., Oestreicher G., Hogue P., Contreiras J., Brandao I. Regulation of succinate dehydrogenase in higher plants. I. Some general characteristics of the membrane-bound enzyme. Plant Physiol. 52:1973;616-621.
    • (1973) Plant Physiol. , vol.52 , pp. 616-621
    • Singer, T.P.1    Oestreicher, G.2    Hogue, P.3    Contreiras, J.4    Brandao, I.5
  • 22
    • 0342597207 scopus 로고
    • Succinate dehydrogenase. A partial purification from mung bean hypocotyls and soybean cotyledons
    • Burke J.J., Siedow J.N., Moreland D.E. Succinate dehydrogenase. A partial purification from mung bean hypocotyls and soybean cotyledons. Plant Physiol. 70:1982;1577-1581.
    • (1982) Plant Physiol. , vol.70 , pp. 1577-1581
    • Burke, J.J.1    Siedow, J.N.2    Moreland, D.E.3
  • 25
    • 0029661903 scopus 로고    scopus 로고
    • 2+ control of respiration in isolated rat liver mitochondria
    • 2+ control of respiration in isolated rat liver mitochondria. Biochemistry. 35:1996;12849-12856.
    • (1996) Biochemistry , vol.35 , pp. 12849-12856
    • Panov, A.1    Scarpa, A.2
  • 26
    • 0025831651 scopus 로고
    • Free fatty acids dissipate proton electrochemical gradients in pea stem microsomes and submitochondrial particles
    • Macrì F., Vianello A., Braidot E., Zancani M. Free fatty acids dissipate proton electrochemical gradients in pea stem microsomes and submitochondrial particles. Biochim. Biophys. Acta. 1058:1991;249-255.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 249-255
    • MacRì, F.1    Vianello, A.2    Braidot, E.3    Zancani, M.4
  • 27
    • 0001767870 scopus 로고
    • Auxin receptor of maize coleoptile membranes do not have ATPase activity?
    • Cross J.M., Briggs R., Dohormann V.C., Rayle P.M. Auxin receptor of maize coleoptile membranes do not have ATPase activity? Plant Physiol. 61:1978;581-584.
    • (1978) Plant Physiol. , vol.61 , pp. 581-584
    • Cross, J.M.1    Briggs, R.2    Dohormann, V.C.3    Rayle, P.M.4
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 11944268830 scopus 로고
    • +-pyrophosphatase. The roles of magnesium, pyrophosphate, and their complexes as substrates, activators, and inhibitors
    • +-pyrophosphatase. The roles of magnesium, pyrophosphate, and their complexes as substrates, activators, and inhibitors. Plant Physiol. 100:1992;1698-1705.
    • (1992) Plant Physiol. , vol.100 , pp. 1698-1705
    • Leigh, R.A.1    Pope, A.J.2    Jennings, I.R.3    Sanders, D.4
  • 31
    • 0000245049 scopus 로고
    • Adenine nucleotide levels in the cytosol, chloroplasts, and mitochondria of wheat leaf protoplasts
    • Stitt M., McC. Lilley R., Heldt H.W. Adenine nucleotide levels in the cytosol, chloroplasts, and mitochondria of wheat leaf protoplasts. Plant Physiol. 70:1982;971-977.
    • (1982) Plant Physiol. , vol.70 , pp. 971-977
    • Stitt, M.1    McC. Lilley, R.2    Heldt, H.W.3
  • 32
    • 0001060481 scopus 로고
    • Adenylate levels, energy charge, and phosphorylation potential during dark-light and light-dark transition in chloroplast, mitochondria, and cytosol of mesophyll protoplasts from Avena sativa L.
    • Hampp R., Goller M., Ziegler H. Adenylate levels, energy charge, and phosphorylation potential during dark-light and light-dark transition in chloroplast, mitochondria, and cytosol of mesophyll protoplasts from Avena sativa L. Plant Physiol. 69:1982;448-455.
    • (1982) Plant Physiol. , vol.69 , pp. 448-455
    • Hampp, R.1    Goller, M.2    Ziegler, H.3
  • 33
    • 0001780038 scopus 로고
    • Carbon metabolism in mitochondria
    • D.T. Dennis, & D.H. Turpin. Harlow: Longman
    • ap Rees T. Carbon metabolism in mitochondria. Dennis D.T., Turpin D.H. Plant Physiology, Biochemistry and Molecular Biology. 1990;106-123 Longman, Harlow.
    • (1990) Plant Physiology, Biochemistry and Molecular Biology , pp. 106-123
    • Ap Rees, T.1
  • 34
    • 0001398314 scopus 로고
    • The use of fura-2 fluorescence to monitor the movement of free calcium ions into the matrix of plant mitochondria
    • Zottini M., Zannoni D. The use of fura-2 fluorescence to monitor the movement of free calcium ions into the matrix of plant mitochondria. Plant Physiol. 102:1993;573-578.
    • (1993) Plant Physiol. , vol.102 , pp. 573-578
    • Zottini, M.1    Zannoni, D.2
  • 35
    • 0017599059 scopus 로고
    • +-potential as a convertible energy source for the living cell
    • +-potential as a convertible energy source for the living cell. FEBS Lett. 74:1977;1-9.
    • (1977) FEBS Lett. , vol.74 , pp. 1-9
    • Skulachev, V.1
  • 36
    • 0024313505 scopus 로고
    • Inorganic pyrophosphate in mitochondrial metabolism
    • Mansurova S.E. Inorganic pyrophosphate in mitochondrial metabolism. Biochim. Biophys. Acta. 977:1989;237-247.
    • (1989) Biochim. Biophys. Acta , vol.977 , pp. 237-247
    • Mansurova, S.E.1
  • 37
    • 0008892546 scopus 로고
    • Effect of inorganic pyrophosphatase on respiration and oxidative phosphorylation in higher plants
    • Kowalczyk S., Maslowski P. Effect of inorganic pyrophosphatase on respiration and oxidative phosphorylation in higher plants. Phytochemistry. 20:1981;2611-2615.
    • (1981) Phytochemistry , vol.20 , pp. 2611-2615
    • Kowalczyk, S.1    Maslowski, P.2
  • 38
    • 0001197431 scopus 로고
    • Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves
    • Weiner H., Stitt M., Heldt H.W. Subcellular compartmentation of pyrophosphate and alkaline pyrophosphatase in leaves. Biochim. Biophys. Acta. 892:1987;13-21.
    • (1987) Biochim. Biophys. Acta , vol.892 , pp. 13-21
    • Weiner, H.1    Stitt, M.2    Heldt, H.W.3
  • 39
    • 0017280603 scopus 로고
    • Molecular and physiological aspects of adenine nucleotide transport in mitochondria
    • Vignais P.V. Molecular and physiological aspects of adenine nucleotide transport in mitochondria. Biochim. Biophys. Acta. 456:1976;1-38.
    • (1976) Biochim. Biophys. Acta , vol.456 , pp. 1-38
    • Vignais, P.V.1


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