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PLANT PHYSIOLOGY , Vol 113, Issue 1 191-199, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Cooperation and Competition between Adenylate Kinase, Nucleoside Diphosphokinase, Electron Transport, and ATP Synthase in Plant Mitochondria Studied by 31P-Nuclear Magnetic Resonance
JKM. Roberts, S. Aubert, E. Gout, R. Bligny and R. Douce
Laboratoire de Physiologie Cellulaire Vegetale, Unite de Recherche Associee 576 Centre National de la Recherche Scientifique (J.K.M.R., S.A., R.B., R.D.), and the Laboratoire de Resonance Magnetique en Biologie et Medecine, Department de Biologie Moleculaire et Structurale (E.G.), CEN-Grenoble, 17 rue des Martyrs 38054, Grenoble Cedex 9, France
Nucleotide metabolism in potato (Solanum tuberosum) mitochondria was
studied using 31P-nuclear magnetic resonance spectroscopy and the O2
electrode. Immediately following the addition of ADP, ATP synthesis
exceeded the rate of oxidative phosphorylation, fueled by succinate
oxidation, due to mitochondrial adenylate kinase (AK) activity two to four
times the maximum activity of ATP synthase. Only when the AK reaction
approached equilibrium was oxidative phosphorylation the primary mechanism
for net ATP synthesis. A pool of sequestered ATP in mitochondria enabled AK
and ATP synthase to convert AMP to ATP in the presence of exogenous
inorganic phosphate. During this conversion, AK activity can indirectly
influence rates of oxidation of both succinate and NADH via changes in
mitochondrial ATP. Mitochondrial nucleoside diphosphokinase, in cooperation
with ATP synthase, was found to facilitate phosphorylation of nucleoside
diphosphates other than ADP at rates similar to the maximum rate of
oxidative phosphorylation. These results demonstrate that plant
mitochondria contain all of the machinery necessary to rapidly regenerate
nucleoside triphosphates from AMP and nucleoside diphosphates made during
cellular biosynthesis and that AK activity can affect both the amount of
ADP available to ATP synthase and the level of ATP regulating electron
transport.
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