1887

Abstract

Summary: Catalase and peroxidase were markedly decreased in quantity in molybdenum-deficient felts of Addition of molybdenum aseptic- ally and to mats deficient in molybdenum restored the activities of the two enzymes and the yield of mycelium to the amounts in the control treatments. Infiltration of hydrogen peroxide to growing felts, deficient in molybdenum, after 3 days of growth, resulted in a partial reconstitution of catalase to 18 % and peroxidase to 50 % of the control levels after a further 2 days growth but the weight of mycelium remained unchanged. There was no positive correlation between the activity of either enzyme at various stages of purification and its molybdenum content as determined by a radioassay method. The purified enzymes were not activated by molybdenum. The effect of molybdenum deficiency on the two iron- containing enzymes is probably indirect, resulting from a decrease in the activity of molybdenum-dependent flavoproteins which produce hydrogen peroxide, the common substrate for catalase and peroxidase.

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1957-12-01
2021-08-01
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References

  1. Feinstein R. N. 1949; Perborate as substrate in a new assay of catalase. J.biol. Chem 180:1197
    [Google Scholar]
  2. Lenhoff H. M., Nicholas D. J. D., Kaplan N. O. 1956; Effects of oxygen, iron, and molybdenum on routes of electron transfer in Pseudomonas fluorescens . J. biol. Chem 220:983
    [Google Scholar]
  3. Lowry O. H., Rosebrough N. L., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. J. biol. Chem 193:265
    [Google Scholar]
  4. Nicholas D. J. D., Fielding A. H. 1951; Use of Aspergillusniger(M) for the determination of magnesium, zinc, copper and molybdenum available in soils to crop plants. J. hort. Sci 26:125
    [Google Scholar]
  5. Nicholas D. J. D. 1952; The use of fungi for determining trace metals in biological materials. Analyst 77:629
    [Google Scholar]
  6. Nicholas D. J. D., Nason A., Mcelroy W. D. 1954; Molybdenum and nitrate reductase. I. Effect of molybdenum on the Neurosporaenzyme. J. biol. Chem 207:341
    [Google Scholar]
  7. Nicholas D. J. D., Nason A. 1954a; Molybdenum and nitrate reductase. II. Molybdenum as a constituent of nitrate reductase. J. biol. Chem 207:353
    [Google Scholar]
  8. Nicholas D. J. D., Nason A. 1954b; Mechanism of action of nitrate reductase from Neurospora . J. biol. Chem 211:183
    [Google Scholar]
  9. Nicholas D. J. D., Nason A. 1954c; Diphosphopyridine-nucleotide-nitrate reductase from Escherichia coli . J. Bact 69:580
    [Google Scholar]
  10. Nicholas D. J. D., Nason A. 1955; Role of molybdenum as a constituent of nitrate reductase from soybean leaves. Plant Physiol 30:135
    [Google Scholar]
  11. Nicholas D. J. D., Stevens H. M. 1955; Valency changes of molybdenum during the enzymatic reduction of nitrate in Neurospora . Nature; Lond.: 1761066
    [Google Scholar]
  12. Nicholas D. J. D. 1956; Effect of molybdenum deficiency on catalase and peroxidase in Neurospora . Nature; Lond.: 178148
    [Google Scholar]
  13. Smith F. G., Robinson W. B., Stotz E. 1949; A colorimetric method for the determination of peroxidase in plant material. J. biol. Chem 179:881
    [Google Scholar]
  14. Theorell H. 1951 In The Enzymes Ed. Sumner J. B., Myrbäck K. 2, i p. 335 New York: Academic Press;
    [Google Scholar]
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