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The main focus of this study was to determine the mechanism by which certain exogenous monovalent salts stimulate rates of net O(2) evolution linked to oxaloacetate reduction in intact spinach chloroplasts. The influence of salts on the dicarboxylate translocator involved in the transport of oxaloacetate and on the activity and activation of the chloroplast enzyme NADP-malate dehydrogenase, which mediates electron transport to oxaloacetate, was examined. High concentrations of KCl (155 millimolar) increased the apparent K(m) for oxaloacetate but did not significantly alter the maximal velocity of uptake. Likewise, external salts (KCl, MgCl(2), or KH(2)PO(4)) had minimal effects on the magnitude of light activation of NADP-malate dehydrogenase. In contrast, measurements of chloroplast NADP-malate dehydrogenase activity (after release by osmotic shock) showed a marked dependence on salt concentration. Rates were stimulated approximately 2-fold by both monovalent (optimally 75 millimolar) and divalent (optimally 20 millimolar) salts. It was inferred that the salt-induced increase in net rates of O(2) evolution linked to oxaloacetate reduction is due, at least in part, to stimulation of NADP-malate dehydrogenase caused by monovalent cation permeability of the chloroplast inner envelope membrane. |
