Premium
Superoxide Dismutase and Unribosylated Cytokinins Interact in the Control of NAD(P)H‐Peroxidation
Author(s) -
Elstner E. F.,
Galek Helena
Publication year - 1988
Publication title -
botanica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 0932-8629
DOI - 10.1111/j.1438-8677.1988.tb00008.x
Subject(s) - nad+ kinase , superoxide dismutase , superoxide , chemistry , peroxidase , biochemistry , dismutase , redox , enzyme , inorganic chemistry
NAD(P)H is rapidly oxidized in the presence of peroxidase, a substituted monophenol such as p ‐coumaric acid, and Mn 2+ ions. As recently reported by Miller (1985), this NAD(P)H oxidation at the expense of molecular oxygen is inhibited by submicromolar concentrations of Cu 2+ ions. This inhibition by cupric ions is counteracted by micromolar concentrations of cytokinins. We now show that NAD(P)H‐oxidation by the above system is under the control of superoxide dismutase, where in the absence of cytokinin‐copper, superoxide dismutase stimulates NAD(P)H‐oxidation. In the presence of unribosylated cytokinins and copper, however, superoxide dismutase acts as an inhibitor. Thus cytokinins and superoxide dismutase may interact in the control of the redox state of plant cells.