Abstract
In heterotrophically grown Scenedesmus obliquus, the specific activity of superoxide dismutase (SOD; EC 1.15.1.1) declined when glucose was abundant, increased as it was depleated, and remained steady at a high level when it was absent. Transition to autotrophic growth produced only a small (20% over 5 d) increase in specific activity above the values obtained in dark-grown cells after glucose and starch-reserve depletion. This small, but consistent, increase did, however, parallel a similar increase in photosynthetic capacity. Polyacrylamide-gel electrophoresis showed the existence of nine isoenzymes of SOD. The three major and one of the minor isoenzymes were present in all extracts while three minor isoenzymes were found only in autotrophically grown cells and two only in heterotrophically grown cells. Characterization studies indicated that two of the major isoenzymes are dimeric FeSODs the other is a tetrameric MnSOD, and of the minor isoenzymes, two are dimeric FeSODs and four are dimeric MnSODs.
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Abbreviations
- SOD:
-
superoxide dismutase
References
Asada, K., Kanematsu, S., Uchida, K. (1977) Superoxide dismutases in photosynthetic organisms: absence of the cuprozinc enzyme in eukaryotic algae. Arch. Biochem. Biophys. 179, 243–256
Asada, K., Nakano, Y. (1978) Affinity for oxygen in photoreduction of molecular oxygen and scavenging of hydrogen peroxide in spinach chloroplasts. Photochem. Photobiol. 28, 917–920
Beauchamp, C., Fridovich, I. (1979) Superoxide dismutase; improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44, 276–287
Britton, L., Malinowski, D.P., Fridovich, I. (1978) Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms. J. Bacteriol. 134, 229–236
Dougherty, H.W., Sadowski, S.J., Baker, E. (1978) A new iron containing superoxide dismutase from Escherichia coli. J. Biol. Chem. 253, 5220–5223
Fridovich, I. (1979) Superoxide and superoxide dismutases. In: Advances in inorganic biochemistry. pp. 67–89, Eichhorn, G.L., Marzilli, L.G., eds. Elsevier/North-Holland, New York
Friedberg, D., Fine, M., Oren, A. (1979) Effect of oxygen on the cyanobacterium Oscillatoria limnetica. Arch. Microbiol. 123, 311–313
Halliwell, B. (1977) The chloroplast at work. A review of modern developments in our understanding of chloroplast metabolism. Prog. Biophys. Mol. Biol. 33, 1–54
Harbour, J.R., Bolton, J.R. (1975) Superoxide formation in spinach chloroplasts: electron spin resonance detection by spin trapping. Biochem. Biophys. Res. Commun. 64, 803–807
Hassan, H.M., Fridovich, I. (1977a) Enzymatic defences against the toxicity of oxygen and streptonigrin in Escherichia coli. J. Bacteriol. 129, 1574–1583
Hassan, H.M., Fridovich, I. (1977b) Regulation of superoxide dismutase in Escherichia coli: glucose effect. J. Bacteriol. 132, 505–510
Hendrick, J.L., Smith, A.J. (1968) Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch. Biochem. Biophys. 126, 155–164
Henry, L.E.A., Hall, D.O. (1977) Superoxide dismutases in green algae: an evolutionary survey. In: Photosynthetic organelles, pp. 377–382, Miyachi, S., Katoh, S., Fujita, Y., Sibata, K., eds. Japanese Society of Plant Physiologists, Japan
Kanematsu, S., Asada, K. (1979) Ferric and manganic superoxide dismutases in Euglena gracilis. Arch. Biochem. Biophys. 195, 535–545
Keele, B.B., Jr., McCord, J.M., Fridovich, I. (1971) Further characterization of bovine superoxide dismutase and its isolation from bovine heart. J. Biol. Chem. 246, 2875–2880
Kessler, E., Authur, W., Brugger, J.E. (1957) The influence of manganese and phosphate on delayed light emission, fluorescence, photoreduction and photosynthesis in algae. Arch. Biochem. Biophys. 71, 326–335
Kirby, J., Blum, J., Kahane, I., Fridovich, I. (1980) Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells. Arch. Biochem. Biophys. 201, 551–555
Lumsden, J., Hall, D.O. (1975) Superoxide dismutase in photosynthetic organisms provides an evolutionary hypothesis. Nature 257, 670–671
Maurer, H.R. (1971) Disc electrophoresis and related techniques of polyacrylamide gel electrophoresis. Walter de Gruyter, Berlin
McCord, J.M., Fridovich, I. (1969) Superoxide dismutase, an enzymatic function for erythrocuprein. J. Biol. Chem. 244, 6049–6055
McCord, J.M., Keele, B.B., Jr., Fridovich, I. (1971) An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc. Natl. Acad. Sci. USA 68, 1024–1027
Mejbaum-Katzenellenbogen W., Dobryszycka, W.M. (1959) New method for quantitative determination of serum proteins separated by paper electrophoresis. Clin. Chim. Acta 4, 515–522
Misra, H.P., Fridovich, I. (1977) Purification and properties of superoxide dismutase from a red alga, Porphyridium cruentum. J. Biol. Chem. 252, 6421–6423
Radmer, R.J., Kok, B. (1976) Photoreduction of O2 primes and replaces CO2 assimilation. Plant Physiol. 58, 336–340
Salin, M.L., Bridges, S.M. (1980) Isolation and characterization of an iron-containing superoxide dismutase from a eukaryote, Brassica campestris. Arch. Biochem. Biophys. 201, 369–374
Tanaka, K., Sugahara, K. (1980) Role of superoxide dismutase in defence against SO2 toxicity and an increase in superoxide dismutase activity with SO2 fumigation. Plant Cell Physiol. 21, 601–611
Von Stein, R.S., Barber, L.E., Hassan, H.M. (1982) Biosynthesis of oxygen-detoxifying enzymes in Bdellovibrio stolpii. J. Bacteriol. 152, 792–796
Weber, K., Osborn, M. (1969) The reliability of molecular weight determinations by dodecyl sulphate polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406–4412
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Redmond, M.J., McEuen, A.R. & Powls, R. Superoxide dismutase in Scenedesmus obliquus . Planta 163, 405–410 (1985). https://doi.org/10.1007/BF00395150
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DOI: https://doi.org/10.1007/BF00395150