Abstract
The kinetics of the cometabolism of trichloroethylene (TCE) by the ammonia-oxidizing soil bacterium Nitrosomonas europaea in short-term (<10-min) incubations were investigated. Three individual effects of TCE cometabolism on this bacterium were characterized. First, we observed that TCE is a potent competitive inhibitor of ammonia oxidation by N. europaea. The K(infi) value for TCE (30 (mu)M) is similar to the K(infm) for ammonia (40 (mu)M). Second, we examined the toxicity associated with TCE cometabolism by N. europaea. Stationary-phase cells of N. europaea oxidized approximately 60 nmol of TCE per mg of protein before ammonia-oxidizing activity was completely inactivated by reactive intermediates generated during TCE oxidation. At the TCE concentrations used in these experiments, ammonia did not provide significant protection against inactivation. Third, we have determined the ability of cells to recover ammonia-oxidizing activity after exposure to TCE. Cells recovering from TCE inactivation were compared with cells recovering from the specific inactivation of ammonia-oxidizing activity by light. The recovery kinetics were indistinguishable when 40% or less of the activity was inactivated. However, at increased levels of inactivation, TCE-inactivated cells did not recover as rapidly as light-inactivated cells. The kinetics of recovery appear to be dependent on both the extent of inactivation of ammonia-oxidizing activity and the degree of specificity of the inactivating treatment.
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- Alvarez-Cohen L., McCarty P. L. Effects of toxicity, aeration, and reductant supply on trichloroethylene transformation by a mixed methanotrophic culture. Appl Environ Microbiol. 1991 Jan;57(1):228–235. doi: 10.1128/aem.57.1.228-235.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Alvarez-Cohen L., McCarty P. L. Product toxicity and cometabolic competitive inhibition modeling of chloroform and trichloroethylene transformation by methanotrophic resting cells. Appl Environ Microbiol. 1991 Apr;57(4):1031–1037. doi: 10.1128/aem.57.4.1031-1037.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Arciero D., Vannelli T., Logan M., Hooper A. B. Degradation of trichloroethylene by the ammonia-oxidizing bacterium Nitrosomonas europaea. Biochem Biophys Res Commun. 1989 Mar 15;159(2):640–643. doi: 10.1016/0006-291x(89)90042-9. [DOI] [PubMed] [Google Scholar]
- Dabrock B., Riedel J., Bertram J., Gottschalk G. Isopropylbenzene (cumene)--a new substrate for the isolation of trichloroethene-degrading bacteria. Arch Microbiol. 1992;158(1):9–13. doi: 10.1007/BF00249058. [DOI] [PubMed] [Google Scholar]
- Dalton H., Stirling D. I. Co-metabolism. Philos Trans R Soc Lond B Biol Sci. 1982 Jun 11;297(1088):481–496. doi: 10.1098/rstb.1982.0056. [DOI] [PubMed] [Google Scholar]
- Ensign S. A., Hyman M. R., Arp D. J. Cometabolic degradation of chlorinated alkenes by alkene monooxygenase in a propylene-grown Xanthobacter strain. Appl Environ Microbiol. 1992 Sep;58(9):3038–3046. doi: 10.1128/aem.58.9.3038-3046.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ensley B. D. Biochemical diversity of trichloroethylene metabolism. Annu Rev Microbiol. 1991;45:283–299. doi: 10.1146/annurev.mi.45.100191.001435. [DOI] [PubMed] [Google Scholar]
- Ewers J., Freier-Schröder D., Knackmuss H. J. Selection of trichloroethene (TCE) degrading bacteria that resist inactivation by TCE. Arch Microbiol. 1990;154(4):410–413. doi: 10.1007/BF00276540. [DOI] [PubMed] [Google Scholar]
- Folsom B. R., Chapman P. J., Pritchard P. H. Phenol and trichloroethylene degradation by Pseudomonas cepacia G4: kinetics and interactions between substrates. Appl Environ Microbiol. 1990 May;56(5):1279–1285. doi: 10.1128/aem.56.5.1279-1285.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fox B. G., Borneman J. G., Wackett L. P., Lipscomb J. D. Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications. Biochemistry. 1990 Jul 10;29(27):6419–6427. doi: 10.1021/bi00479a013. [DOI] [PubMed] [Google Scholar]
- Hyman M. R., Arp D. J. 14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase. J Biol Chem. 1992 Jan 25;267(3):1534–1545. [PubMed] [Google Scholar]
- Hyman M. R., Murton I. B., Arp D. J. Interaction of Ammonia Monooxygenase from Nitrosomonas europaea with Alkanes, Alkenes, and Alkynes. Appl Environ Microbiol. 1988 Dec;54(12):3187–3190. doi: 10.1128/aem.54.12.3187-3190.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hyman M. R., Wood P. M. Methane oxidation by Nitrosomonas europaea. Biochem J. 1983 Apr 15;212(1):31–37. doi: 10.1042/bj2120031. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hyman M. R., Wood P. M. Suicidal inactivation and labelling of ammonia mono-oxygenase by acetylene. Biochem J. 1985 May 1;227(3):719–725. doi: 10.1042/bj2270719. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Keener W. K., Arp D. J. Kinetic Studies of Ammonia Monooxygenase Inhibition in Nitrosomonas europaea by Hydrocarbons and Halogenated Hydrocarbons in an Optimized Whole-Cell Assay. Appl Environ Microbiol. 1993 Aug;59(8):2501–2510. doi: 10.1128/aem.59.8.2501-2510.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Malachowsky K. J., Phelps T. J., Teboli A. B., Minnikin D. E., White D. C. Aerobic mineralization of trichloroethylene, vinyl chloride, and aromatic compounds by rhodococcus species. Appl Environ Microbiol. 1994 Feb;60(2):542–548. doi: 10.1128/aem.60.2.542-548.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Oldenhuis R., Oedzes J. Y., van der Waarde J. J., Janssen D. B. Kinetics of chlorinated hydrocarbon degradation by Methylosinus trichosporium OB3b and toxicity of trichloroethylene. Appl Environ Microbiol. 1991 Jan;57(1):7–14. doi: 10.1128/aem.57.1.7-14.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rasche M. E., Hicks R. E., Hyman M. R., Arp D. J. Oxidation of monohalogenated ethanes and n-chlorinated alkanes by whole cells of Nitrosomonas europaea. J Bacteriol. 1990 Sep;172(9):5368–5373. doi: 10.1128/jb.172.9.5368-5373.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rasche M. E., Hyman M. R., Arp D. J. Factors Limiting Aliphatic Chlorocarbon Degradation by Nitrosomonas europaea: Cometabolic Inactivation of Ammonia Monooxygenase and Substrate Specificity. Appl Environ Microbiol. 1991 Oct;57(10):2986–2994. doi: 10.1128/aem.57.10.2986-2994.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rasche Madeline E., Hyman Michael R., Arp Daniel J. Biodegradation of Halogenated Hydrocarbon Fumigants by Nitrifying Bacteria. Appl Environ Microbiol. 1990 Aug;56(8):2568–2571. doi: 10.1128/aem.56.8.2568-2571.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vannelli T., Logan M., Arciero D. M., Hooper A. B. Degradation of halogenated aliphatic compounds by the ammonia- oxidizing bacterium Nitrosomonas europaea. Appl Environ Microbiol. 1990 Apr;56(4):1169–1171. doi: 10.1128/aem.56.4.1169-1171.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vogel T. M., McCarty P. L. Biotransformation of tetrachloroethylene to trichloroethylene, dichloroethylene, vinyl chloride, and carbon dioxide under methanogenic conditions. Appl Environ Microbiol. 1985 May;49(5):1080–1083. doi: 10.1128/aem.49.5.1080-1083.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wackett L. P., Brusseau G. A., Householder S. R., Hanson R. S. Survey of microbial oxygenases: trichloroethylene degradation by propane-oxidizing bacteria. Appl Environ Microbiol. 1989 Nov;55(11):2960–2964. doi: 10.1128/aem.55.11.2960-2964.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wackett L. P., Gibson D. T. Degradation of trichloroethylene by toluene dioxygenase in whole-cell studies with Pseudomonas putida F1. Appl Environ Microbiol. 1988 Jul;54(7):1703–1708. doi: 10.1128/aem.54.7.1703-1708.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]