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Plant Physiology 55:1023-1030 (1975)
© 1975 American Society of Plant Biologists

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Articles

The Glyceraldehyde 3-Phosphate and Glycerate 3-Phosphate Shuttle and Carbon Dioxide Assimilation in Intact Spinach Chloroplasts 1

Elchanan S. Bamberger2, Barry A. Ehrlich3 and Martin Gibbs

a Department of Biology, Brandeis University, Waltham, Massachusetts 02154

The regulation of CO2 assimilation by intact spinach (Spinacia oleracea) chloroplasts by exogenous NADP-linked nonreversible D-glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9) was investigated. This dehydrogenase mediated a glyceraldehyde 3-phosphate/glycerate 3-phosphate shuttle for the indirect transfer of NADPH from chloroplast to the external medium. The rate of NADPH formation in the medium reflected glyceraldehyde 3-phosphate efflux from the chloroplast. Increasing enzyme concentrations stimulated NADP reduction and, in turn, CO2 fixation. Pyrophosphate increased CO2 fixation by apparently inhibiting glyceraldehyde 3-phosphate efflux. Increasing the glycerate 3-phosphate concentration above 0.1 mM stimulated glyceraldehyde 3-phosphate efflux but inhibited CO2 fixation. Addition of up to 0.5 mM orthophosphate enhanced both glyceraldehyde 3-phosphate efflux and CO2 fixation while each was inhibited by higher orthophosphate concentrations. The mechanism by which the extent of glyceraldehyde 3-phosphate efflux regulated the rate of CO2 fixation in chloroplasts was discussed.

2 Present address: Department of Biology, University of Haifa, The School of Education, Oranim, Israel.

3 Present address: Medical School, Tufts University, Boston, Mass.

1 This research was supported by National Science Foundation Grant GB29126X2 and by National Institutes of Health Institutional Grant GM-1586-07.






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Copyright © 1975 by the American Society of Plant Biologists