Sucrose concentration in phloem sap was several times higher than in the cytosol of mesophyll cells. The results suggest that phloem loading involves active steps in the analyzed tree species. Phloem loading in source leaves is a key step for carbon partitioning and passive symplastic loading has been proposed for several tree species. However, experimental evidence to prove the potential for sucrose diffusion from mesophyll to phloem is rare. Here, we analyzed three tree species (two angiosperms, Fagus sylvatica, Magnolia kobus, and one gymnosperm, Gnetum gnemon) to investigate the proposed phloem loading mechanism. For this purpose, the minor vein structure and the sugar concentrations in phloem sap as well as in the subcellular compartments of mesophyll cells were investigated. The analyzed tree species belong to the open type minor vein subcategory. The sucrose concentration in the cytosol of mesophyll cells ranged between 75 and 165 mM and was almost equal to the vacuolar concentration. Phloem sap could be collected from F. sylvatica and M. kobus and the concentration of sucrose in phloem sap was about five- and 11-fold higher, respectively, than in the cytosol of mesophyll cells. Sugar exudation of cut leaves was decreased by p-chloromercuribenzenesulfonic acid, an inhibitor of sucrose-proton transporter. The results suggest that phloem loading of sucrose in the analyzed tree species involves active steps, and apoplastic phloem loading seems more likely.

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A molecular-level understanding of the effects of atmospheric-pressure plasma on biological samples requires knowledge of the effects on proteins. Superoxide dismutases, which detoxify superoxide under oxidative stress conditions, play a key role in bacterial plasma resistance. Investigation of the impact of dielectric barrier discharge (DBD) treatment on purified superoxide dismutases SodA and SodB of Escherichia coli showed that DBD treatment caused a rapid protein degradation, with only 8% of protein remaining after 10 min. The affinity of SodA for the metal cofactor Mn 2+ was reduced. Mass spectrometry, in conjunction with coupledcluster calculations, revealed that modifications of amino acid residues in the active site can explain the decreased metal affinity and a distortion of the coordination geometry responsible for the activity loss.