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Effects of Aminoacetonitrile on Net Photosynthesis, Ribulose-1,5-Bisphosphate Levels, and Glycolate Pathway Intermediates
Author(s) -
Elisabeth Créach,
Cecil R. Stewart
Publication year - 1982
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.70.5.1444
Subject(s) - photorespiration , glyoxylate cycle , photosynthesis , chemistry , rubisco , ribulose , glycine , pyruvate carboxylase , biochemistry , enzyme , metabolism , amino acid
The effects of aminoacetonitrile (a competitive inhibitor of glycine oxidation) on net photosynthesis, glycolate pathway intermediates, and ribulose-1,5-bisphosphate (RuBP) levels have been investigated at different O(2) and CO(2) concentrations with soybean (Glycine max)[L] Merr. cv Pioneer 1677) leaf discs floated on 25 millimolar aminoacetonitrile (AAN) for 50 minutes prior to assay.At 2% O(2) and 200 or 330 microliters per liter CO(2), the inhibitor had no effect on the rate of net photosynthesis and RuBP levels when compared with the control levels. At 11% to 60% O(2), AAN caused a decrease in net photosynthesis in addition to the inhibition by O(2). This extra inhibition ranged from 22% to 59% depending on the O(2) and CO(2) concentrations. The levels of RuBP, however, were 1.3 to 2.7 times higher than in the control plants at the same O(2) concentrations. At 40% O(2) and 200 microliters per liter CO(2), the inhibitor caused a 6-fold increase in glycine and more than 2-fold increase in glyoxylate levels, whereas those of glycolate decreased by approximately one-half.The decrease in net photosynthesis observed with AAN is not the result of the depletion of the RuBP pool due to the lack of recycling of carbon from the glycolate pathway to the Calvin cycle. The higher levels of RuBP caused by AAN in photorespiratory conditions, suggest that RuBP carboxylase was inhibited. Glyoxylate could be a possible candidate for the inhibition of the enzyme but what is known so far about its inhibitory properties in vitro may not fit the existing in vivo conditions. An alternative explanation for the inhibition is proposed.

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