Is Root Catalase a Bifunctional Catalase-Peroxidase?

Antioxidants (Basel). 2017 May 25;6(2):39. doi: 10.3390/antiox6020039.


Plant catalases exhibit spatial and temporal distribution of their activity. Moreover, except from the typical monofunctional catalase, a bifunctional catalase-peroxidase has been reported. The aim of this study was to investigate whether the leaf and root catalases from six different plant species (Lactuca sativa, Cichorium endivia, Apium graveolens, Petroselinum crispum, Lycopersicon esculentum, and Solanum melongena) correspond to the monofunctional or the bifunctional type based on their sensitivity to the inhibitor 3-amino-1,2,4-triazole (3-AT). The leaf catalases from all species seem to be monofunctional since they are very sensitive to 3-AT. On the other hand, the root enzymes from Lactuca sativa, Cichorium endivia, Lycopersicon esculentum, and Solanum melongena seem to be bifunctional catalase-peroxidases, considering that they are relatively insensitive to 3-AT, whereas the catalases from Apium graveolens and Petroselinum crispum display the same monofunctional characteristics as the leaves' enzymes. The leaf catalase activity is usually higher (Lactuca sativa, Petroselinum crispum, and Solanum melongena) or similar (Cichorium endivia and Apium graveolens) to the root one, except for the enzyme from Lycopersicon esculentum, while in all plant species the leaf protein concentration is significantly higher than the root protein concentration. These results suggest that there are differences between leaf and root catalases-differences that may correspond to their physiological role.

Keywords: aminotriazole; catalase; leaf; peroxidase; root.