Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 67:467-469 (1981)
© 1981 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (44)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Journet, E.-P.
Right arrow Articles by Douce, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Journet, E.-P.
Right arrow Articles by Douce, R.
Agricola
Right arrow Articles by Journet, E.-P.
Right arrow Articles by Douce, R.
Articles

Role of Glutamate-oxaloacetate Transaminase and Malate Dehydrogenase in the Regeneration of NAD+ for Glycine Oxidation by Spinach leaf Mitochondria 1

Etienne-Pascal Journet, Michel Neuburger and Roland Douce

Physiologie Cellulaire Végétale, Département de Recherche Fondamentale/Biologie Végétale, Centre d'Etudes Nucléaires et Université Scientifique et Médicale de Grenoble, 85X 38041 Grenoble Cedex, France

During glycine oxidation by spinach leaf mitochondria, oxygen consumption showed a strong and transient inhibition upon addition of oxaloacetate or aspartate plus {alpha}-ketoglutarate. During the course of the inhibition, aspartate and {alpha}-ketoglutarate were stoichiometrically transformed into malate and glutamate.

It is concluded that oxaloacetate formed by transamination is reduced by the malate dehydrogenase, which allows the regeneration of NAD+ for glycine oxidation and, thus, by-passes the respiratory chain. Efficiency of a malate-glutamate/aspartate-{alpha}-ketoglutarate shuttle upon illumination and under in vivo conditions is discussed.


1 Supported in part by a research grant from the Centre National de la Recherche Scientifique (ERA 847: Interactions Plastes-Cytoplasme-Mitochondries).




This article has been cited by other articles:


Home page
Mol. Cell. ProteomicsHome page
C. P. Lee, H. Eubel, N. O'Toole, and A. H. Millar
Heterogeneity of the Mitochondrial Proteome for Photosynthetic and Non-photosynthetic Arabidopsis Metabolism
Mol. Cell. Proteomics, July 1, 2008; 7(7): 1297 - 1316.
[Abstract] [Full Text] [PDF]


Home page
J Exp BotHome page
G. Noctor, G. Queval, and B. Gakiere
NAD(P) synthesis and pyridine nucleotide cycling in plants and their potential importance in stress conditions
J. Exp. Bot., May 1, 2006; 57(8): 1603 - 1620.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
W. Shen, Y. Wei, M. Dauk, Y. Tan, D. C. Taylor, G. Selvaraj, and J. Zou
Involvement of a Glycerol-3-Phosphate Dehydrogenase in Modulating the NADH/NAD+ Ratio Provides Evidence of a Mitochondrial Glycerol-3-Phosphate Shuttle in Arabidopsis
PLANT CELL, February 1, 2006; 18(2): 422 - 441.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
I. Hanning, K. Baumgarten, K. Schott, and H. W. Heldt
Oxaloacetate Transport into Plant Mitochondria
Plant Physiology, March 1, 1999; 119(3): 1025 - 1032.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1981 by the American Society of Plant Biologists