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Plant Physiology 55:12-14 (1975)
© 1975 American Society of Plant Biologists

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Articles

Effect of Disalicylidenepropanediamine on the Light-dependent Reduction of Carbon Dioxide and Glycerate 3-Phosphate in Intact Spinach Chloroplasts 1

J. Michael Robinson2, Erwin Latzko3 and Martin Gibbs

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

Disalicylidenepropanediamine (DSPD) at 0.1 to 1 mM levels inhibited light-dependent 14CO2 assimilation in intact spinach chloroplasts about 50 to 80%, and this inhibition was accompanied by an increased ratio of 14C-glycerate 3-phosphate to 14C-glyceraldehyde 3-phosphate. Enzymatic analysis established that DSPD also inhibited the light-dependent reduction of glycerate 3-phosphate in intact spinach chloroplasts. DSPD at 0.5 mM did not inhibit ribose 5-phosphate isomerase, ribulose 5-phosphate kinase, glycerate 3-phosphate kinase, NADP+-linked glyceraldehyde 3-phosphate dehydrogenase or ribulose 1,5-diphosphate carboxylase. The inhibition of chloroplast 14CO2 assimilation by DSPD appeared to be related to the inhibition of the photosynthetic electron transport chain. These observations are consistent with experimental results which demonstrated that DSPD inhibited directly the chloroplast lamellar membrane-mediated, light-dependent reduction of ferredoxin (Trebst, A. and M. Burba, 1967, Z. Pflanzenphysiol. 57: 419-433 and Ben-Amotz, A. and M. Avron, 1972, Plant Physiol. 49: 244-248).

2 National Institute of Health Trainee, Grant GM-1586-07.

3 Permanent address: Institut für Chemie und Landwirtscharftl. Technologie, 805 Weihenstephan, West Germany.

1 This research was supported by United States Atomic Energy Commission Grant AT 11-1 (3231).






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Copyright © 1975 by the American Society of Plant Biologists