Abstract
The biochemical response of the microorganisms Lipomyces starkeyi (Lod & Rij), Escherichia coli K-12 W3110, Bacillus subtilis 168 (Marburg) and Pseudomonas sp. strain TTO1 to the presence of growth-inhibitory concentrations of paraquat was studied. Paraquat was added to each culture at a concentration previously determined to reduce the culture growth rate by up to 50%. The changes in activity of a number of enzymes previously shown to be associated with the defense of the mammalian system against the action of paraquat were studied. While the response of E. coli was in agreement with that found in other studies of this microorganism and supports a commonly accepted mechanism for paraquat toxicity, the results obtained with L. starkeyi, B. subtilis, and Pseudomonas sp. strain TTO1 suggest that other mechanisms exist for protection against the toxicity of paraquat.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Autor A. P. Reduction of paraquat toxicity by superoxide dismutase. Life Sci. 1974 Apr 1;14(7):1309–1319. doi: 10.1016/0024-3205(74)90439-1. [DOI] [PubMed] [Google Scholar]
- Bus J. S., Aust S. D., Gibson J. E. Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity. Biochem Biophys Res Commun. 1974 Jun 4;58(3):749–755. doi: 10.1016/s0006-291x(74)80481-x. [DOI] [PubMed] [Google Scholar]
- Bus J. S., Cagen S. Z., Olgaard M., Gibson J. E. A mechanism of paraquat toxicity in mice and rats. Toxicol Appl Pharmacol. 1976 Mar;35(3):501–513. doi: 10.1016/0041-008x(76)90073-9. [DOI] [PubMed] [Google Scholar]
- Carr R. J., Bilton R. F., Atkinson T. Mechanism of biodegradation of paraquat by Lipomyces starkeyi. Appl Environ Microbiol. 1985 May;49(5):1290–1294. doi: 10.1128/aem.49.5.1290-1294.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cuatrecasas P. Membrane receptors. Annu Rev Biochem. 1974;43(0):169–214. doi: 10.1146/annurev.bi.43.070174.001125. [DOI] [PubMed] [Google Scholar]
- Gage J. C. The action of paraquat and diquat on the respiration of liver cell fractions. Biochem J. 1968 Oct;109(5):757–761. doi: 10.1042/bj1090757. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gregory E. M., Fridovich I. Induction of superoxide dismutase by molecular oxygen. J Bacteriol. 1973 May;114(2):543–548. doi: 10.1128/jb.114.2.543-548.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gregory E. M., Fridovich I. Oxygen toxicity and the superoxide dismutase. J Bacteriol. 1973 Jun;114(3):1193–1197. doi: 10.1128/jb.114.3.1193-1197.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gregory E. M., Goscin S. A., Fridovich I. Superoxide dismutase and oxygen toxicity in a eukaryote. J Bacteriol. 1974 Feb;117(2):456–460. doi: 10.1128/jb.117.2.456-460.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gregory E. M., Yost F. J., Jr, Fridovich I. Superoxide dismutases of Escherichia coli: intracellular localization and functions. J Bacteriol. 1973 Sep;115(3):987–991. doi: 10.1128/jb.115.3.987-991.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli. J Bacteriol. 1977 Mar;129(3):1574–1583. doi: 10.1128/jb.129.3.1574-1583.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds. Arch Biochem Biophys. 1979 Sep;196(2):385–395. doi: 10.1016/0003-9861(79)90289-3. [DOI] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical. J Biol Chem. 1979 Nov 10;254(21):10846–10852. [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Superoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli. J Biol Chem. 1978 Nov 25;253(22):8143–8148. [PubMed] [Google Scholar]
- Huotari F. I., Nelson T. E., Smith F., Kirkwood S. Purification of an exo-beta-D-(1 bonded to 3)-glucanase from Basidiomycete species QM 806. J Biol Chem. 1968 Mar 10;243(5):952–956. [PubMed] [Google Scholar]
- Ilett K. F., Stripp B., Menard R. H., Reid W. D., Gillette J. R. Studies on the mechanism of the lung toxicity of paraquat: comparison of tissue distribution and some biochemical parameters in rats and rabbits. Toxicol Appl Pharmacol. 1974 May;28(2):216–226. doi: 10.1016/0041-008x(74)90007-6. [DOI] [PubMed] [Google Scholar]
- Kong S., Davison A. J. The role of interactions between O2, H2O2, .OH,e- and O2- in free radical damage to biological systems. Arch Biochem Biophys. 1980 Oct 1;204(1):18–29. doi: 10.1016/0003-9861(80)90003-x. [DOI] [PubMed] [Google Scholar]
- Kornbrust D. J., Mavis R. D. The effect of paraquat on microsomal lipid peroxidation in vitro and in vivo. Toxicol Appl Pharmacol. 1980 Apr;53(2):323–332. doi: 10.1016/0041-008x(80)90433-0. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Manzo L., Gregotti C., Di Nucci A., Richelmi P. Toxicology of paraquat and related bipyridyls: biochemical, clinical and therapeutic aspects. Vet Hum Toxicol. 1979 Dec;21(6):404–410. [PubMed] [Google Scholar]
- McCord J. M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem. 1969 Nov 25;244(22):6049–6055. [PubMed] [Google Scholar]
- Moustafa Hassan H., Fridovich I. Regulation of superoxide dismutase synthesis in Escherichia coli: glucose effect. J Bacteriol. 1977 Nov;132(2):505–510. doi: 10.1128/jb.132.2.505-510.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Omura T., Takesue S. A new method for simultaneous purification of cytochrome b5 and NADPH-cytochrome c reductase from rat liver microsomes. J Biochem. 1970 Feb;67(2):249–257. doi: 10.1093/oxfordjournals.jbchem.a129248. [DOI] [PubMed] [Google Scholar]
- Paglia D. E., Valentine W. N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med. 1967 Jul;70(1):158–169. [PubMed] [Google Scholar]
- Rose M. S., Smith L. L., Wyatt I. Evidence for energy-dependent accumulation of paraquat into rat lung. Nature. 1974 Nov 22;252(5481):314–315. doi: 10.1038/252314b0. [DOI] [PubMed] [Google Scholar]
- Rose M. S., Smith L. L., Wyatt I. The relevance of pentose phosphate pathway stimulation in rat lung to the mechanism of paraquat toxicity. Biochem Pharmacol. 1976 Aug 1;25(15):1763–1767. doi: 10.1016/0006-2952(76)90412-3. [DOI] [PubMed] [Google Scholar]
- Simons R. S., Jackett P. S., Carroll M. E., Lowrie D. B. Superoxide independence of paraquat toxicity in Escherichia coli. Toxicol Appl Pharmacol. 1976 Aug;37(2):271–280. doi: 10.1016/0041-008x(76)90090-9. [DOI] [PubMed] [Google Scholar]
- Witschi H., Kacew S., Hirai K. I., Côté M. G. In vivo oxidation of reduced nicotinamide-adenine dinucleotide phosphate by paraquat and diquat in rat lung. Chem Biol Interact. 1977 Nov;19(2):143–160. doi: 10.1016/0009-2797(77)90027-8. [DOI] [PubMed] [Google Scholar]
