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. 1985 Apr;77(4):851–856. doi: 10.1104/pp.77.4.851

Photorespiration-Induced Reduction of Ribulose Bisphosphate Carboxylase Activation Level 1

Chris J Chastain 1,2, William L Ogren 1,2
PMCID: PMC1064618  PMID: 16664149

Abstract

Leaf photosynthesis and ribulose bisphosphate carboxylase activation level were inhibited in several mutants of the C3 crucifer Arabidopsis thaliana which possess lesions in the photorespiratory pathway. This inhibition occurred when leaves were illuminated under a photorespiratory atmosphere (50% O2, 350 microliters per liter CO2, balance N2), but not in nonphotorespiratory conditions (2% O2, 350 microliters per liter CO2, balance N2). Inhibition of carboxylase activation level was observed in strains with deficient glycine decarboxylase, serine transhydroxymethylase, serine-glyoxylate aminotransferase, glutamate synthase, and chloroplast dicarboxylate transport activities, but inhibition did not occur in a glycolate-P phosphatase-deficient strain. Also, the photorespiration inhibitor aminoacetonitrile produced a decline in leaf and protoplast ribulose bisphosphate carboxylase activation level, but was without effect on intact chloroplasts. Fructose bisphosphatase, a light-activated enzyme which is strongly dependent on stromal pH and Mg2+ for regulation, was unaffected by conditions which caused inhibition of ribulose bisphosphate carboxylase. Thus, the mechanism of inhibition does not appear to involve changes in stromal Mg2+ and pH but rather is associated with metabolite flux through the photorespiratory pathway.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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