alexa Effect of inland salt-alkaline stress on C4 enzymes, pigments, antioxidant enzymes, and photosynthesis in leaf, bark, and branch chlorenchyma of poplars


Biochemistry & Analytical Biochemistry

Author(s): H M Wang, W J Wang, H Z Wang, Y Wang, H N Xu, Y G Zu

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The effects of soil salt-alkaline (SA) stress on leaf physiological processes are well studied in the laboratory, but less is known about their effect on leaf, bark and branch chlorenchyma and no reports exist on their effect on C4 enzymes in field conditions. Our results demonstrated that activities of C4 enzymes, such as phospholenolpyruvate carboxylase (PEPC), NADP-malic enzyme (NADP-ME), pyruvate orthophosphate dikinase (PPDK), and NADP-dependent malate dehydrogenase (NADP-MDH), could also be regulated by soil salinity/alkalinity in poplar (Populus alba × P. berolinensis) trees, similarly as the already documented changes in activities of antioxidative enzymes, such as superoxide dismutase (SOD), catalase (CAT), and glutathione reductase (GR), pigment composition, photosynthesis, and respiration. However, compared with 50–90% changes in a leaf and young branch chlorenchyma, much smaller changes in malondialdehyde (MDA), antioxidative enzymes, and C4 enzymatic activities were observed in bark chlorenchyma, showing that the effect of soil salinity/alkalinity on enzymatic activities was organ-dependent. This suggests that C4 enzymatic ratios between nonleaf chlorenchyma and leaf (the commonly used parameter to discern the operation of the C4 photosynthetic pathway in nonleaf chlorenchyma), were dependent on SA stress. Moreover, much smaller enhancement of these ratios was seen in an improved soil contrary to SA soil, when the fresh mass (FM) was used as the unit compared with a calculation on a chlorophyll (Chl) unit. An identification of the C4 photosynthesis pathway via C4 enzyme difference between chlorenchyma and leaf should take this environmental regulation and unit-based difference into account.

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This article was published in Photosynthetica and referenced in Biochemistry & Analytical Biochemistry

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