The glyceraldehyde 3-phosphate and glycerate 3-phosphate shuttle and carbon dioxide assimilation in intact spinach chloroplasts.
The regulation of CO(2) 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, CO(2) fixation. Pyrophosphate increased CO(2) 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 CO(2) fixation. Addition of up to 0.5 mm orthophosphate enhanced both glyceraldehyde 3-phosphate efflux and CO(2) fixation while each was inhibited by higher orthophosphate concentrations. The mechanism by which the extent of glyceraldehyde 3-phosphate efflux regulated the rate of CO(2) fixation in chloroplasts was discussed.
Bamberger
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Department of Biology, Brandeis University, Waltham, Massachusetts 02154.
Ehrlich
B A
BA
Gibbs
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