Hydrogen Peroxide Production is a General Property of the Lignifying Xylem from Vascular Plants

Production of hydrogen peroxide (H₂O₂) by the lignifying xylemof several vascular plants has been studied using a new histochemicalmethod based on the H₂O₂-dependent oxidation of 3,5,3'5'-tetramethylbenzidine(TMB) catalysed by cell wall peroxidases. This method allowsH₂O₂to be determined in the range of 5–100 µM, whereother methods, such as the KI/starch reagent, fail. With thismethod, it has been possible to determine H₂O₂production inthe lignifying xylem of a wide range of vascular plants (gymnospermsand angiosperms). The capability of xylem tissues of sustainingH₂O₂production lends support to the hypothesis that cinnamylalcohol polymerization in xylem vessels is caused by an H₂O₂-dependentoxidative coupling process.Copyright 1998 Annals of Botany Company H₂O₂generation, lignification, peroxidase, tetramethylbenzidine, xylem.     

The Decarboxylative Pathway of lndole-3-Acetic Acid Catabolism Is not Functional in Grapevine Protoplasts

The functionality of the decarboxylative pathway of indole-3-aceticacid (IAA) was studied in both suspension-cultured cells andprotoplasts of grapevine (Vitis vinifera cv. Gamay) throughfeeding experiments with labelled IAA. The results showed that,although cells and protoplasts were capable of taking IAA fromthe media, the ability to oxidize IAA was restricted to thecell wall of cultured cells. These results suggest that thedecarboxylative pathway of IAA catabolism does not functionin grapevine protoplasts and they are discussed in relationto the co-localization of peroxidase (EC 1.11.1.7 [EC] ) and anthocyani(di)nsin vacuoles. This lack of function is presumably favoured bya strong compartmentalization (i.e. accumulation by a factorof 730) of IAA in the cytoplasm compared to vacuoles. Key words: Indole-3-acetic acid catabolism, anthocyani(di)ns, peroxidase, protoplasts     

A Biochemical and Cytochemical Study of the Cuticle-associated Peroxidases in Lupinus

A biochemical and cytochemical study of peroxidases (EC 1.11.1.7 [EC] )associated with the outermost cell layers of Lupinus albus hypocotylshas been performed. Cytochemical investigations showed thatin the epidermis of lupin hypocotyls, peroxidatic activitiescould be detected mainly at the level of the endoplasmic reticulum,Golgi apparatus, ground substance of the cytoplasm, intercellularspaces between adjacent epidermal cells, and in the cuticlelayer. No peroxidatic reactions were seen at the level of eitherthe radial or the tangential walls. The cuticle peroxidaticreaction was due to two acidic isoperoxidases, also found incell walls of vascular tissues, and was further characterizedthrough a study of its catalytic activities. These studies showedthat cuticle-associated peroxidases were able to oxidize genistein,but unable to oxidize ascorbic acid. These results suggest thatextracellular peroxidases associated with the outermost celllayers of lupin hypocotyls are involved more in the metabolismof isoflavones of the cuticle layer than in the growth responsesof the whole organ. Epidermal cell, cuticle, peroxidase cytochemistry, genistein oxidation, Lupinus albus     

The vacuolar localization of a basic peroxidase isoenzyme responsible for the synthesis of α-31,41-anhydrovinblastine in Catharanthus roseus (L.) G. Don Leaves

Partially purified protein extracts of Catharanthus roseus leaves were able to couple catharanthine and vindoline to produce α-3′,4′-anhydrovinblastine (AVLB) in a reaction strictly dependent on H₂O₂. This result, and the co-purification of peroxidase with AVLB synthetase activity, strongly suggest a peroxidase-like nature for the coupling enzyme. Only one peroxidase isoenzyme was detected in C. roseus leaves, and it was shown that this isoenzyme consists of a molecularly-heterogeneous basic peroxidase (EC 1-11-1-7) mainly located in the vacuole. These results suggest that a basic peroxidase located in the vacuole may be the main enzyme responsible for AVLB synthesis in C. roseus leaves. This isoenzyme was also found in cell walls where a peroxidase inhibitor was detected.