Premium
The relationship between the activity of various iron‐containing and iron‐free enzymes and the presence of nicotianamine in tomato seedlings
Author(s) -
Pich Axel,
Scholz Günter
Publication year - 1993
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1993.tb01775.x
Subject(s) - aconitase , lycopersicon , enzyme , peroxidase , chemistry , biochemistry , catalase , enzyme assay , phosphoenolpyruvate carboxylase , dehydrogenase , wild type , mutant , botany , biology , gene
The influence of nicotianamine (NA) and iron on the activities of 4 iron‐containing and two iron‐free enzymes in leaves and roots of the NA‐free tomato mutant chloronerva and its NA‐containing wild‐type ( Lycopersicon esculentum Mill. cv. Bonner Beste) was investigated. Aconitase (EC 4.2.1.3) activity in both leaves and roots was much higher in the mutant under normal iron supply (10 μ M FeEDTA) and in wild‐type under iron deficiency than in wild‐type supplied with 10 μ M FeEDTA. Application of NA to chloronerva leaves led to a decrease of aconitase activity in leaves and roots. NA had no effect on the enzyme activity when added to the assay medium. Similar results were obtained for the iron‐containing enzymes catalase (EC 1.11.1.6), ascorbate‐dependent peroxidase (EC 1.11.1.11) and guaiacol‐dependent peroxidase (EC 1.11.1.7) in roots. NA treatment of the mutant leaves decreased enzyme activities in roots down to wild‐type values. In vivo NA application had no effect on enzyme activities in leaf extracts. The activities of the iron‐free enzymes NAD + ‐malate dehydrogenase (EC 1.1.1.37) and phosphofructokinase (EC 2.7.1.11) in root and leaf extracts were not influenced by the iron supply to the plants.