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Plant Physiology 95:1131-1137 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Redox Transfer across the Inner Chloroplast Envelope Membrane 1

Dieter Heineke, Burgi Riens, Heike Grosse, Petra Hoferichter, Ute Peter, Ulf-Ingo Flügge2 and Hans Walter Heldt

Institut für Biochemie der Pflanze, Universität Göttingen, Untere Karspüle 2, 3400 Göttingen, Federal Republic of Germany

In leaves of spinach plants (Spinacia oleracea L.) grown in ambient CO2 the subcellular contents of adenylates, pyridine nucleotides, 3-phosphoglycerate, dihydroxyacetone phosphate, malate, glutamate, 2-oxoglutarate, and aspartate were assayed in the light and in the dark by nonaqueous fractionation technique. From the concentrations of NADP and NADPH determined in the chloroplast fraction of illuminated leaves the stromal NADPH to NADP ratio is calculated to be 0.5. For the cytosol a NADH to NAD ratio of 10–3 is calculated from the assay of the concentrations of NAD, malate, glutamate, aspartate, and 2-oxoglutarate on the assumption that the reactions catalyzed by the cytosolic glutamate oxaloacetate transaminase and malate dehydrogenase are not far away from equilibrium. For the transfer of redox equivalents from the chloroplastic NADPH to the cytosolic NAD two metabolite shuttles are operating across the inner envelope membrane: the triosephosphate-3-phosphoglycerate shuttle and the malate-oxaloacetate shuttle. Although both shuttles would have the capacity to level the redox state of the stromal and cytosolic compartment, this apparently does not occur. To gain an insight into the regulatory processes we calculated the free energy of the enzymic reactions and of the translocation steps involved. From the results it is concluded that the triosephosphate-3-phosphoglycerate shuttle is mainly controlled by the chloroplastic reaction of 3-phosphoglycerate reduction and of the cytosolic reaction of triosephosphate oxidation. The malate-oxaloacetate shuttle is found to be regulated by the chloroplastic NADP-malate dehydrogenase and also by the translocating step across the envelope membrane.

2 Present address: Lehrstuhl Botanik I, Universität Würzburg, Mittlerer Dallenbergweg 64, 8700 Würzburg (FRG).

1 Supported by the Deutsche Forschungsgemeinschaft (H. W. H.).




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