Open AccessPoly-β-hydroxybutyrate Utilization by Soybean (Glycine max Merr.) Nodules and Assessment of Its Role in Maintenance of Nitrogenase Activity
Author(s) -
Peter P. Wong,
Harold J. Evans
Publication year - 1971
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.47.6.750
Subject(s) - nitrogenase , glycine , biochemistry , isocitrate dehydrogenase , carbohydrate , nodule (geology) , biology , enzyme , isocitrate lyase , incubation , hydrolysis , nitrogen fixation , bacteria , amino acid , glyoxylate cycle , paleontology , genetics
Soybean (Glycine max) nodule bacteroids contain high concentrations of poly-beta-hydroxybutyrate and possess a depolymerase system that catalyzes the hydrolysis of the polymer. Changes in poly-beta-hydroxybutyrate content and in activities of nitrogenase, beta-hydroxybutyrate dehydrogenase, and isocitrate lyase in nodule bacteroids were investigated under conditions in which the supply of carbohydrate from the soybean plants was interrupted. The poly-beta-hydroxybutyrate content of bacteroids did not decrease appreciably until the carbohydrate supply from the host plants was limited by incubation of excised nodules, incubation of plants in the dark, or by senescence of the host plant. Isocitrate lyase activity in bacteroids was not detected until poly-beta-hydroxybutyrate utilization appeared to begin. The presence of a supply of poly-beta-hydroxybutyrate in nodule bacteroids was not sufficient for maintenance of high nitrogenase activity under conditions of limited carbohydrate supply from the host plant. An unusually high activity of beta-hydroxybutyrate dehydrogenase was observed in bacteroid extracts but no significant change in the activity of this enzyme was observed as a result of apparent utilization of poly-beta-hydroxybutyrate by nodule bacteroids.