The role of monovalent cations for photosynthesis of isolated intact chloroplasts
- PMID: 24306249
- DOI: 10.1007/BF00380879
The role of monovalent cations for photosynthesis of isolated intact chloroplasts
Abstract
The role of monovalent cations in the photosynthesis of isolated intact spinach chloroplasts was investigated. When intact chloroplasts were assayed in a medium containing only low concentrations of mono- and divalent cations (about 3 mval l(-1)), CO2-fixation was strongly inhibited although the intactness of chloroplasts remained unchanged. Addition of K(+), Rb(+), or Na(+) (50-100 mM) fully restored photosynthesis. Both the degree of inhibition and restoration varied with the plant material and the storage time of the chloroplasts in "low-salt" medium. In most experiments the various monovalent cations showed a different effectiveness in restoring photosynthesis of low-salt chloroplasts (K(+)>Rb(+)>Na(+)). Of the divalent cations tested, Mg(2+) also restored photosynthesis, but to a lesser extent than the monovalent cations.In contrast to CO2-fixation, reduction of 3-phosphoglycerate was not ihibited under low-salt conditions. In the dark, CO2-fixation of lysed chloroplasts supplied with ATP, NADPH, and 3-phosphoglycerate strictly required the presence of Mg(2+) but was independent of monovalent cations. This finding excludes a direct inactivation of Calvin cycle enzymes as a possible basis for the inhibition of photosynthesis under low-salt conditions.Light-induced alkalization of the stroma and an increase in the concentration of freely exchangeable Mg(2+) in the stroma, which can be observed in normal chloroplasts, did not occur under low-salt conditions but were strongly enhanced after addition of monovalent cations (50-100 mM) or Mg(2+) (20-50 mM).The relevance of a light-triggered K(+)/H(+) exchange at the chloroplast envelope is discussed with regard to the light-induced increase in the pH and the Mg(2+) concentration in the stroma, which are thought to be obligatory for light activation of Calvincycle enzymes.