Abstract
Leaves and nodules (bacteroids and cytosol) of alfalfa (Medicago sativa L. cv Aragon) plants inoculated with Rhizobium meliloti strain 102F51 have been analyzed for the presence of the enzymes superoxide dismutase (SOD, EC 1.15.1.1), catalase (EC 1.11.1.6), and peroxidase (EC 1.11.1.7). All three fractions investigated (leaves, bacteroids, and nodular cytosol) show Cu,Zn-SOD activity. Besides, the bacteroids and cytosol of nodules possess CN−-insensitive SOD activities. Studies of SOD inactivation with H2O2 indicate that, very likely, a Mn-SOD is present in the bacteroids, and suggest that the cytosol contain both Mn-SOD and Fe-SOD. Bacteroids show high catalase activity but lack peroxidase. By contrast, the nodule cytosol exhibits an elevated peroxidase activity as compared with the foliar tissue; this activity was completely inhibited by 50 to 100 micromolar KCN. The significantly lower contents of H2O2 and malondialdehyde (a product of lipid peroxidation) in nodules with respect to those in leaves reveal that the above-mentioned bacteroid and cytosol enzymes act in an efficient and combined manner to preserve integrity of nodule cell membranes and to keep leghemoglobin active.
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- Asada K., Yoshikawa K., Takahashi M., Maeda Y., Enmanji K. Superoxide dismutases from a blue-green alga, Plectonema boryanum. J Biol Chem. 1975 Apr 25;250(8):2801–2807. [PubMed] [Google Scholar]
- Bannister J. V., Bannister W. H. Isolation and characterization of superoxide dismutase. Methods Enzymol. 1984;105:88–93. doi: 10.1016/s0076-6879(84)05012-6. [DOI] [PubMed] [Google Scholar]
- Beauchamp C. O., Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochim Biophys Acta. 1973 Jul 12;317(1):50–64. doi: 10.1016/0005-2795(73)90198-0. [DOI] [PubMed] [Google Scholar]
- Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
- Bridges S. M., Salin M. L. Distribution of iron-containing superoxide dismutase in vascular plants. Plant Physiol. 1981 Aug;68(2):275–278. doi: 10.1104/pp.68.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Francis A. J., Alexander M. Catalase activity and nitrogen fixation in legume root nodules. Can J Microbiol. 1972 Jun;18(6):861–864. doi: 10.1139/m72-132. [DOI] [PubMed] [Google Scholar]
- Fridovich I. Superoxide dismutases. Annu Rev Biochem. 1975;44:147–159. doi: 10.1146/annurev.bi.44.070175.001051. [DOI] [PubMed] [Google Scholar]
- Fridovich I. The biology of oxygen radicals. Science. 1978 Sep 8;201(4359):875–880. doi: 10.1126/science.210504. [DOI] [PubMed] [Google Scholar]
- Giannopolitis C. N., Ries S. K. Superoxide dismutases: I. Occurrence in higher plants. Plant Physiol. 1977 Feb;59(2):309–314. doi: 10.1104/pp.59.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Job D., Zeba B., Puppo A., Rigaud J. Kinetic studies of the reaction of ferric soybean leghemoglobins with hydrogen peroxide, cyanide and nicotinic acid. Eur J Biochem. 1980 Jun;107(2):491–500. doi: 10.1111/j.1432-1033.1980.tb06055.x. [DOI] [PubMed] [Google Scholar]
- Martin J. P., Jr, Fridovich I. Evidence for a natural gene transfer from the ponyfish to its bioluminescent bacterial symbiont Photobacter leiognathi. The close relationship between bacteriocuprein and the copper-zinc superoxide dismutase of teleost fishes. J Biol Chem. 1981 Jun 25;256(12):6080–6089. [PubMed] [Google Scholar]
- McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
- Patterson B. D., MacRae E. A., Ferguson I. B. Estimation of hydrogen peroxide in plant extracts using titanium(IV). Anal Biochem. 1984 Jun;139(2):487–492. doi: 10.1016/0003-2697(84)90039-3. [DOI] [PubMed] [Google Scholar]
- Puget K., Michelson A. M. Isolation of a new copper-containing superoxide dismutase bacteriocuprein. Biochem Biophys Res Commun. 1974 Jun 4;58(3):830–838. doi: 10.1016/s0006-291x(74)80492-4. [DOI] [PubMed] [Google Scholar]
- Puppo A., Rigaud J., Job D., Ricard J., Zeba B. Peroxidase content of soybean root nodules. Biochim Biophys Acta. 1980 Aug 7;614(2):303–312. doi: 10.1016/0005-2744(80)90220-x. [DOI] [PubMed] [Google Scholar]
- Salin M. L., Bridges S. M. Isolation and characterization of an iron-containing superoxide dismutase from a eucaryote, Brassica campestris. Arch Biochem Biophys. 1980 May;201(2):369–374. doi: 10.1016/0003-9861(80)90524-x. [DOI] [PubMed] [Google Scholar]