Abstract
Mutants sensitive to moderate H2O2 concentrations were selected in a HfrphoA (S33)Escherichia coli strain after mutagenesis withN-methyl,N′-nitro,N-nitrosoguanidine (NG). Of the sensitive strains, 31% were catalase-deficient and retained glutathione reductase levels similar to those of the parental strain, whereas 69% still had normal catalase and glutathione reductase activities. Mutants supersensitive to low H2O2 concentrations were selected in a catalase-deficient strain (CGR201) after mutagenesis with NG. Of these, 20% were glutathione reductase-deficient, and the remaining 80% were unaffected in this enzymatic activity. Compared with the parental strain S33, H2O2 was 5 to 12 times more toxic for the sensitive mutants, and 19 to 21 times for the supersensitive ones.
Similar content being viewed by others
Literature Cited
Bachman, B. J., Low, K. B. 1980. Linkage map ofEscherichia coli K-12, edition 6. Microbiological Reviews44:1–56.
Beers, R. F. Jr., Sizer, I. W. 1952. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. Journal of Biological Chemistry195:133–139.
Chance, B., Boveris, A., Nakase, Y., Sies, H. 1978. Hydroperoxide metabolism: an overview, pp 95–106. In: Sies, H., Wendel, A. (eds.), Functions of glutathione in liver and kidney, Berlin: Springer-Verlag.
Cohen, G., Hochstein, P. 1963. Glutathione peroxidase: the primary agent for the elimination of hydrogen peroxide in erythrocytes. Biochemistry2:1420–1427.
Davis, N. K., Greer, S., Jones-Mortimer, M. C., Perham, R. N. 1982. Isolation and mapping of glutathione reductase-negative mutants ofEscherichia coli K 12. Journal of General Microbiology128:1631–1634.
Green, M. H. L., Muriel, W. J. 1976. Mutagen testing using Trp+ reversion inEscherichia coli. Mutation Research38:3–32.
Jones, D. P., Eklow, L., Thor, H., Orrenius, S. 1981. Metabolism of hydrogen peroxide in isolated hepatocytes: relative contributions of catalase and glutathione peroxidase in decomposition of endogenously generated H2O2. Archives of Biochemistry and Biophysics210:505–516.
Levine, S. A. 1977. Isolation and characterization of catalase deficient mutants ofSalmonella typhimurium. Molecular and General Genetics150:205–209.
Lopez-Barea, J., Lee, C. Y. 1979. Mouse-liver glutathione reductase. Purification, kinetics and regulation. European Journal of Biochemistry98:487–499.
Lowry, O. H., Rosebrough, M. J., Farr, A. L., Randall, R. J. 1951. Protein measurements with the Folin-phenol reagent. Journal of Biological Chemistry193:265–275.
Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor: Cold Spring Harbor Laboratory.
Mills, G. C. 1957. I. Glutathione peroxidase, an enzyme which protects hemoglobin from oxidative breakdown. Journal of Biological Chemistry229:189–197.
Swarup-Mitra, S. 1977. Activity of glutathione peroxidase and glutathione reductase in G-6-PD deficient subjects. Indian Journal of Medical Research66:253–259.
Yamazaki, I. 1974. Peroxidase. pp. 535–558. In: Hayaishi, O. (ed.) Molecular mechanisms of oxygen activation. New York: Academic Press.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Barbado, C., Ramírez, M., Blanco, M.A. et al. Mutants ofEscherichia coli sensitive to hydrogen peroxide. Current Microbiology 8, 251–253 (1983). https://doi.org/10.1007/BF01577723
Issue Date:
DOI: https://doi.org/10.1007/BF01577723