Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1979 Jul;38(1):29–34. doi: 10.1128/aem.38.1.29-34.1979

Bovine superoxide dismutase and copper ions potentiate the bactericidal effect of autoxidizing cysteine.

G K Nyberg, G P Granberg, J Carlsson
PMCID: PMC243430  PMID: 573589

Abstract

When cysteine is oxidized by oxygen, hydrogen peroxide is formed, and hydrogen peroxide is very toxic to Peptostreptococcus anaerobius VPI 4330-1. Native and inactivated superoxide dismutase increased the rate of oxidation of cysteine and thereby potentiated the toxic effect of cysteine. A similar increase in the rate of oxidation of cysteine and in the toxicity of cysteine was obtained with Cu2+.

Full text

PDF
29

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Avigad G. An NADH coupled assay system for galactose oxidase. Anal Biochem. 1978 Jun 1;86(2):470–476. doi: 10.1016/0003-2697(78)90771-6. [DOI] [PubMed] [Google Scholar]
  2. BARRY V. C., CONALTY M. L., DENNENY J. M., WINDER F. Peroxide formation in bacteriological media. Nature. 1956 Sep 15;178(4533):596–597. doi: 10.1038/178596a0. [DOI] [PubMed] [Google Scholar]
  3. Bhuyan K. C., Bhuyan D. K. Superoxide dismutase of the eye: relative functions of superoxide dismutase and catalase in protecting the ocular lens from oxidative damage. Biochim Biophys Acta. 1978 Aug 3;542(1):28–38. doi: 10.1016/0304-4165(78)90229-5. [DOI] [PubMed] [Google Scholar]
  4. Boveris A., Martino E., Stoppani A. O. Evaluation of the horseradish peroxidase-scopoletin method for the measurement of hydrogen peroxide formation in biological systems. Anal Biochem. 1977 May 15;80(1):145–158. doi: 10.1016/0003-2697(77)90634-0. [DOI] [PubMed] [Google Scholar]
  5. Carlsson J., Granberg G. P., Nyberg G. K., Edlund M. B. Bactericidal effect of cysteine exposed to atmospheric oxygen. Appl Environ Microbiol. 1979 Mar;37(3):383–390. doi: 10.1128/aem.37.3.383-390.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Carlsson J., Nyberg G., Wrethén J. Hydrogen peroxide and superoxide radical formation in anaerobic broth media exposed to atmospheric oxygen. Appl Environ Microbiol. 1978 Aug;36(2):223–229. doi: 10.1128/aem.36.2.223-229.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cavallini D., De Marco C., Duprè S., Rotilio G. The copper catalyzed oxidation of cysteine to cystine. Arch Biochem Biophys. 1969 Mar;130(1):354–361. doi: 10.1016/0003-9861(69)90044-7. [DOI] [PubMed] [Google Scholar]
  8. Cohen G., Somerson N. L. Catalase-aminotriazole method for measuring secretion of hydrogen peroxide by microorganisms. J Bacteriol. 1969 May;98(2):543–546. doi: 10.1128/jb.98.2.543-546.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Dempsey P. M., O'Leary J., Condon S. Polarographic assay of hydrogen peroxide accumulation in microbial cultures. Appl Microbiol. 1975 Feb;29(2):170–174. doi: 10.1128/am.29.2.170-174.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fridovich I. The biology of oxygen radicals. Science. 1978 Sep 8;201(4359):875–880. doi: 10.1126/science.210504. [DOI] [PubMed] [Google Scholar]
  11. Frölander F., Carlsson J. Bactericidal effect of anaerobic broth exposed to atmospheric oxygen tested on Peptostreptococcus anaerobius. J Clin Microbiol. 1977 Aug;6(2):117–123. doi: 10.1128/jcm.6.2.117-123.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Gaitonde M. K. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J. 1967 Aug;104(2):627–633. doi: 10.1042/bj1040627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Gregory E. M., Fridovich I. Oxygen metabolism in Lactobacillus plantarum. J Bacteriol. 1974 Jan;117(1):166–169. doi: 10.1128/jb.117.1.166-169.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Halliwell B. Biochemical mechanisms accounting for the toxic action of oxygen on living organisms: the key role of superoxide dismutase. Cell Biol Int Rep. 1978 Mar;2(2):113–128. doi: 10.1016/0309-1651(78)90032-2. [DOI] [PubMed] [Google Scholar]
  15. Harmon S. M., Kautter D. A. Recovery of clostridia on catalase-treated plating media. Appl Environ Microbiol. 1977 Apr;33(4):762–770. doi: 10.1128/aem.33.4.762-770.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry. 1975 Dec 2;14(24):5299–5303. doi: 10.1021/bi00695a011. [DOI] [PubMed] [Google Scholar]
  17. Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry. 1975 Dec 2;14(24):5294–5299. doi: 10.1021/bi00695a010. [DOI] [PubMed] [Google Scholar]
  18. MARGOLIASH E., NOVOGRODSKY A., SCHEJTER A. Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase. Biochem J. 1960 Feb;74:339–348. doi: 10.1042/bj0740339. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Martin S. E., Flowers R. S., Ordal Z. J. Catalase: its effect on microbial enumeration. Appl Environ Microbiol. 1976 Nov;32(5):731–734. doi: 10.1128/aem.32.5.731-734.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. McCord J. M., Keele B. B., Jr, Fridovich I. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proc Natl Acad Sci U S A. 1971 May;68(5):1024–1027. doi: 10.1073/pnas.68.5.1024. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Olsen J., Davis L. The oxidation of dithiothreitol by peroxidases and oxygen. Biochim Biophys Acta. 1976 Sep 14;445(2):324–329. doi: 10.1016/0005-2744(76)90086-3. [DOI] [PubMed] [Google Scholar]
  22. PROOM H., WOIWOD A. J., BARNES J. M., ORBELL W. G. A growth-inhibitory effect on Shigella dysenteriae which occurs with some batches of nutrient agar and is associated with the production of peroxide. J Gen Microbiol. 1950 May;4(2):270–276. doi: 10.1099/00221287-4-2-270. [DOI] [PubMed] [Google Scholar]
  23. TAKAGI T., ISEMURA T. ACCELERATING EFFECT OF COPPER ION ON THE REACTIVATION OF REDUCED TAKA-AMYLASE A THROUGH CATALYSIS OF THE OXIDATION OF SULFHYDRYL GROUPS. J Biochem. 1964 Oct;56:344–350. doi: 10.1093/oxfordjournals.jbchem.a127999. [DOI] [PubMed] [Google Scholar]
  24. Wyss O., Clark J. B., Haas F., Stone W. S. The Role of Peroxide in the Biological Effects of Irradiated Broth. J Bacteriol. 1948 Jul;56(1):51–57. [PMC free article] [PubMed] [Google Scholar]
  25. Yamada T., Carlsson J. Regulation of lactate dehydrogenase and change of fermentation products in streptococci. J Bacteriol. 1975 Oct;124(1):55–61. doi: 10.1128/jb.124.1.55-61.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES