Activity and Compartmentation of Photosynthetic Carboxylases in Normal and Chloroplast-mutant Maize Leaves

The activity of ribulose-l,5-diphosphate carboxylase (RudiP-carboxylase) and phosphoenolpyruvate carboxylase (PEP-carboxylase) measured in vitro was independent from the chlorophyll content of the leaves. The relatively high activity of PEP-carboxylase as compared to the RudiP-carboxylase activity was particularly pronounced in the mutants. Realization of the potential (in vitro measured) carboxylating activities in fixation of CO₂in vivo was practically complete in normal leaves. In the mutants, however, CO₂ fixation was lower than the level permitted by the carboxylase activity. This could be explained only in part by the impaired rate of photophosphorylation. Compartmentation of PEP-carboxylase was different in normal and mutant leaves: in contrast to the normal ones, parenchyma-sheath cells of the mutants exhibited high PEP-carboxylase activity. Competition of PEP-carboxylase with RudiP-carboxylase for CO₂ in the mutants led to accumulation of organic acids, and can account for their low photosynthetic activity.