1887

Abstract

The partially purified monodehydroascorbate reductase (EC 1.6.5.4) from Z showed a pH optimum of 7·0 and a temperature optimum of 41 °C, and had an of 52000. Activity was threefold higher with NADPH than with N ADH; the values for N ADPH and NADH were 7 and 210 μm, respectively. The partially purified dehydroascorbate reductase (EC 1.8.5.1) had a pH optimum of 7·0, a temperature optimum of 38 °C and an of 28000. The enzyme was specific for reduced glutathione as an electron donor, with a of 0·85 m, and for dehydroascorbate, with a of 0·26 m. The enzyme reaction proceeded in either an ordered or a random manner. Both reductases were markedly inhibited by thiol inhibitors, and the inhibition was overcome by thiol compounds such as 2-mercaptoethanol and dithiothreitol. Both reductases were cytosolic. The activities of monodehydroascorbate and dehydroascorbate reductases could account for the regeneration of ascorbate from monodehydroascorbate and dehydroascorbate produced by ascorbate peroxidase (EC 1.11.1.11) for scavenging hydrogen peroxide.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-133-2-227
1987-02-01
2024-04-26
Loading full text...

Full text loading...

/deliver/fulltext/micro/133/2/mic-133-2-227.html?itemId=/content/journal/micro/10.1099/00221287-133-2-227&mimeType=html&fmt=ahah

References

  1. Arrigoni O., Dipierro S., Borraccino G. 1981; Ascorbate free radical reductase, a key enzyme of the ascorbic acid system. FEBS Letters 125:242–244
    [Google Scholar]
  2. Beevers H. 1954; The oxidation of reduced diphos- phopyridine nucleotide by an ascorbate system from cucumber. Plant Physiology 29:265–269
    [Google Scholar]
  3. Bigley R., Riddle M., Layman D., Stankova L. 1981; Human cell dehydroascorbate reductase: kinetic and functional properties. Biochimica et biophysica acta 659:15–22
    [Google Scholar]
  4. De Duve C., Pressman B. C., Gianetto R., Wattiaux T. G. 1955; Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver. Biochemical Journal 60:604–617
    [Google Scholar]
  5. Foyer C. H., Halliwell B. 1977; Purification and properties of dehydroascorbate reductase from spinach leaves. Phytochemistry 16:1347–1350
    [Google Scholar]
  6. Hossain M. A., Asada K. 1984; Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. Plant and Cell Physiology 25:85–92
    [Google Scholar]
  7. Hossain M. A., Asada K. 1985; Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme. Journal of Biological Chemistry 260:12920–12926
    [Google Scholar]
  8. Hossain M. A., Nakano Y., Asada K. 1984; Monodehydroascorbate reductase in spinach chloro- plasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide. Plant and Cell Physiology 25:385–395
    [Google Scholar]
  9. Isegawa Y., Nakano Y., Kitaoka S. 1984; Submitochondrial location and some properties of NAD+- and NADP+-linked malate dehydrogenase in Euglena . Agricultural and Biological Chemistry 48:549–552
    [Google Scholar]
  10. Ito A., Hayashi A., Yoshida T. 1981; Participation of a cytochrome b-like hemoprotein of outer mitochondrial membrane (OM cytochrome b) in NADH-semidehydroascorbic acid reductase activity of rat liver. Biochemical and Biophysical Research Communications 101:591–598
    [Google Scholar]
  11. Koren L. E., Hutner S. H. 1967; High-yield media for photosynthesizing Euglena gracilis Z. Journal of Protozoology 14: suppl. 17
    [Google Scholar]
  12. Mapson L. W. 1967; Biochemical systems. In The Vitamins I pp. 386–398 Sebrell W. H. Jr Harris R. S. Edited by New York: Academic Press;
    [Google Scholar]
  13. Nason A., Wosilait W. D., Terrell A. J. 1954; The enzymic oxidation of reduced pyridine nucleotides by an oxidation product of ascorbic acid. Archives of Biochemistry and Biophysics 48:233–235
    [Google Scholar]
  14. Oda Y., Miyatake K., Nakano Y., Kitaoka S. 1981; Subcellular location and some properties of isocitrate dehydrogenase isoenzymes in Euglena gracilis . Agricultural and Biological Chemistry 45:2619–2621
    [Google Scholar]
  15. Rabinowitz H., Reisfeld A., Sagher D., Edelman M. 1975; Ribulose bisphosphate carboxylase from autotrophic Euglena gracilis . Plant Physiology 56:345–350
    [Google Scholar]
  16. Schulze H. U., Staudinger H. 1971; Lipid dependency of NADH: semidehydroascorbic acid oxidoreductase (EC 1.6.5.4). Hoppe-Seyler’s Zeitschrift für physiologische Chemie 352:309–317
    [Google Scholar]
  17. Schulze H. U., Schott H. H., Staudinger H. 1972; Isolierung und Charakterisierung einer NADH-Semidehydroascorbinsaure-oxidoreduktase aus Neurospora crassa . Hoppe-Seyler’s Zeitschrift für physiologische Chemie 353:1931–1942
    [Google Scholar]
  18. Shigeoka S., Yokota A., Nakano Y., Kitaoka S. 1979a; The effect of illumination on the l-ascorbic acid content in Euglena gracilis Z. Agricultural and Biological Chemistry 43:2053–2058
    [Google Scholar]
  19. Shigeoka S., Nakano Y., Kitaoka S. 1979b; Some properties and subcellular localization of l- gulono-γ-lactone dehydrogenase in Euglena gracilis Z. Agricultural and Biological Chemistry 43:2187–2188
    [Google Scholar]
  20. Shigeoka S., Nakano Y., Kitaoka S. 1980a; Occurrence of l-ascorbic acid in Euglena gracilis Z . Bulletin of University of Osaka Prefecture, Series B32:43–48
    [Google Scholar]
  21. Shigeoka S., Nakano Y., Kitaoka S. 1980b; Metabolism of hydrogen peroxide in Euglena gracilis Z by l-ascorbic acid peroxidase. Biochemical Journal 186:377–380
    [Google Scholar]
  22. Shigeoka S., Nakano Y., Kitaoka S. 1980c; Purification and some properties of l-ascorbic acid- specific peroxidase in Euglena gracilis Z. Archives of Biochemistry and Biophysics 201:121–127
    [Google Scholar]
  23. Smillie R. M. 1968; Enzymology of Euglena . In The Biology of Euglena II pp. 1–54 Buetow D. E. Edited by New York & London: Academic Press;
    [Google Scholar]
  24. Tokunaga M., Nakano Y., Kitaoka S. 1976; Separation and properties of the NAD-linked and NADP-linked isozymes of succinic semialdehyde dehydrogenase in Euglena gracilis Z. Biochimica et biophysica acta 429:55–62
    [Google Scholar]
  25. Tokunaga M., Nakano Y., Kitaoka S. 1979; Subcellular localization of the G AB A-shunt enzymes in Euglena gracilis strain Z. Journal of Protozoology 26:471–473
    [Google Scholar]
  26. Yamaguchi M., Joslin M. A. 1952; Purification and properties of dehydroascorbic acid reductase of peas (Pisum sativum). Archives of Biochemistry and Biophysics 38:451–465
    [Google Scholar]
  27. Yamazaki I., Piette L. H. 1961; Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions. Biochimica et biophysica acta 50:62–69
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-133-2-227
Loading
/content/journal/micro/10.1099/00221287-133-2-227
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error