Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1995 Apr;107(4):1209–1216. doi: 10.1104/pp.107.4.1209

Effects of Temperature on Infected Cell O2 Concentration and Adenylate Levels in Attached Soybean Nodules.

M M Kuzma 1, A F Topunov 1, D B Layzell 1
PMCID: PMC157254  PMID: 12228427

Abstract

To assess the role of O2 in the regulation of nodule metabolism following a decrease or an increase in temperature, the fractional oxygenation of leghemoglobin (FOL) was measured in soybean (Glycine max L. Merr.) nodules during rapid and gradual changes in temperature from 20[deg]C to either 15 or 25[deg]C. The affinity of leghemoglobin for O2 was also measured at each temperature and the values were used to calculate the infected cell O2 concentration (Oi). After nodules were transferred to 15[deg]C, FOL and Oi increased and adenylate energy charge (AEC = [ATP + 0.5ADP]/[ATP + ADP + AMP]) increased from 0.70 to 0.78. The temperature increase was associated with a decrease in FOL and Oi. We concluded that changes in nodule temperature alter the respiratory demand of the nodules for O2, resulting in a change in Oi and a shift in the balance between ATP consumption and ATP production within the nodule tissue.

Full Text

The Full Text of this article is available as a PDF (830.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Almeida M. R., Altland K., Rauh S., Gawinowicz M., Moreira P., Costa P. P., Saraiva M. J. Characterization of a basic transthyretin variant--TTR Arg 102--in the German population. Biochim Biophys Acta. 1991 Oct 21;1097(3):224–226. doi: 10.1016/0925-4439(91)90039-c. [DOI] [PubMed] [Google Scholar]
  2. Appleby C. A., Bradbury J. H., Morris R. J., Wittenberg B. A., Wittenberg J. B., Wright P. E. Leghemoglobin. Kinetic, nuclear magnetic resonance, and optical studies of pH dependence of oxygen and carbon monoxide binding. J Biol Chem. 1983 Feb 25;258(4):2254–2259. [PubMed] [Google Scholar]
  3. Del Castillo L. D., Hunt S., Layzell D. B. The Role of Oxygen in the Regulation of Nitrogenase Activity in Drought-Stressed Soybean Nodules. Plant Physiol. 1994 Nov;106(3):949–955. doi: 10.1104/pp.106.3.949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Del Castillo L. D., Layzell D. B. Drought Stress, Permeability to O2 Diffusion, and the Respiratory Kinetics of Soybean Root Nodules. Plant Physiol. 1995 Apr;107(4):1187–1194. doi: 10.1104/pp.107.4.1187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Denison R. F., Layzell D. B. Measurement of legume nodule respiration and o(2) permeability by noninvasive spectrophotometry of leghemoglobin. Plant Physiol. 1991 May;96(1):137–143. doi: 10.1104/pp.96.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gibson Q. H., Wittenberg J. B., Wittenberg B. A., Bogusz D., Appleby C. A. The kinetics of ligand binding to plant hemoglobins. Structural implications. J Biol Chem. 1989 Jan 5;264(1):100–107. [PubMed] [Google Scholar]
  7. Imamura T., Riggs A. Equilibria and kinetics of ligand binding by leghemoglobin from soybean root nodules. J Biol Chem. 1972 Jan 25;247(2):521–526. [PubMed] [Google Scholar]
  8. Kuzma M. M., Hunt S., Layzell D. B. Role of Oxygen in the Limitation and Inhibition of Nitrogenase Activity and Respiration Rate in Individual Soybean Nodules. Plant Physiol. 1993 Jan;101(1):161–169. doi: 10.1104/pp.101.1.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kuzma M. M., Layzell D. B. Acclimation of Soybean Nodules to Changes in Temperature. Plant Physiol. 1994 Sep;106(1):263–270. doi: 10.1104/pp.106.1.263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Oresnik I. J., Layzell D. B. Composition and Distribution of Adenylates in Soybean (Glycine max L.) Nodule Tissue. Plant Physiol. 1994 Jan;104(1):217–225. doi: 10.1104/pp.104.1.217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Quast R., Vesterberg O. Isoelectric focusing and separation of hemoglobins of Myxine glutinosa L. in a natural pH gradient. Acta Chem Scand. 1968;22(5):1499–1508. doi: 10.3891/acta.chem.scand.22-1499. [DOI] [PubMed] [Google Scholar]
  12. Saari L. L., Klucas R. V. Nonenzymatic reduction of ferric leghemoglobin. Biochim Biophys Acta. 1987 Apr 8;912(2):198–202. doi: 10.1016/0167-4838(87)90089-6. [DOI] [PubMed] [Google Scholar]
  13. di Prisco G., Condò S. G., Tamburrini M., Giardina B. Oxygen transport in extreme environments. Trends Biochem Sci. 1991 Dec;16(12):471–474. doi: 10.1016/0968-0004(91)90182-u. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES