Abstract
The effect in vivo of high nutrient levels of copper (240 micromolar) on the activity of different metalloenzymes containing Cu, Mn, Fe, and Zn, distributed in chloroplasts, peroxisomes, and mitochondria, was studied in leaves of two varieties of Pisum sativum L. plants with different sensitivity to copper. The metalloenzymes studied were: cytochrome c oxidase, Mn-superoxide dismutase (Mn-SOD) and Cu,Zn-superoxide dismutase I (Cu,Zn-SOD I), for mitochondria; catalase and Mn-SOD, for peroxisomes; and isozyme Cu,Zn-SOD II for chloroplasts. The activity of mitochondrial SOD isozymes (Mn-SOD and Cu,Zn-SOD I) was very similar in Cu-tolerant and Cu-sensitive plants, whereas cytochrome c oxidase was lower in Cu-sensitive plants. Chloroplastid Cu,Zn-SOD activity was the same in the two plant varieties. In contrast, the peroxisomal Mn-SOD activity was considerably higher in Cu-tolerant than in Cu-sensitive plants, and the activity of catalase was also increased in peroxisomes of Cu-tolerant plants. The higher activities of these peroxisomal active oxygen-related enzymes in Cu-tolerant plants suggest the involvement of reactive oxygen intermediates (O2−, OH) in the mechanism of Cu lethality, and also imply a function for peroxisomal Mn-SOD in the molecular mechanisms of plant tolerance to Cu in Pisum sativum L.
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- Aebi H. Catalase in vitro. Methods Enzymol. 1984;105:121–126. doi: 10.1016/s0076-6879(84)05016-3. [DOI] [PubMed] [Google Scholar]
- Arnon D. I. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949 Jan;24(1):1–15. doi: 10.1104/pp.24.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [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]
- Pugh S. Y., DiGuiseppi J. L., Fridovich I. Induction of superoxide dismutases in Escherichia coli by manganese and iron. J Bacteriol. 1984 Oct;160(1):137–142. doi: 10.1128/jb.160.1.137-142.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sandmann G., Böger P. Copper-mediated Lipid Peroxidation Processes in Photosynthetic Membranes. Plant Physiol. 1980 Nov;66(5):797–800. doi: 10.1104/pp.66.5.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schmitt M. R., Edwards G. E. Isolation and purification of intact peroxisomes from green leaf tissue. Plant Physiol. 1982 Oct;70(4):1213–1217. doi: 10.1104/pp.70.4.1213. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schnarrenberger C., Oeser A., Tolbert N. E. Development of Microbodies in Sunflower Cotyledons and Castor Bean Endosperm during Germination. Plant Physiol. 1971 Nov;48(5):566–574. doi: 10.1104/pp.48.5.566. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwitzguebel J. P., Siegenthaler P. A. Purification of peroxisomes and mitochondria from spinach leaf by percoll gradient centrifugation. Plant Physiol. 1984 Jul;75(3):670–674. doi: 10.1104/pp.75.3.670. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sevilla F., López-Gorgé J., Del Río L. A. Characterization of a Manganese Superoxide Dismutase from the Higher Plant Pisum sativum. Plant Physiol. 1982 Nov;70(5):1321–1326. doi: 10.1104/pp.70.5.1321. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thornalley P. J., Vasák M. Possible role for metallothionein in protection against radiation-induced oxidative stress. Kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim Biophys Acta. 1985 Jan 21;827(1):36–44. doi: 10.1016/0167-4838(85)90098-6. [DOI] [PubMed] [Google Scholar]
- Wagner G. J. Characterization of a cadmium-binding complex of cabbage leaves. Plant Physiol. 1984 Nov;76(3):797–805. doi: 10.1104/pp.76.3.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weisiger R. A., Fridovich I. Superoxide dismutase. Organelle specificity. J Biol Chem. 1973 May 25;248(10):3582–3592. [PubMed] [Google Scholar]
- del Río L. A., Sandalio L. M., Youngman R. J., Elstner E. F. Percoll reversibly inhibits superoxide dismutase. Rev Esp Fisiol. 1985 Sep;41(3):351–355. [PubMed] [Google Scholar]