Skip to main content
NCBI home page
Environmental Health Perspectives logoLink to Environmental Health Perspectives
. 1985 Dec;64:151–170. doi: 10.1289/ehp.8564151

Chemistry and biology of spin-trapping radicals associated with halocarbon metabolism in vitro and in vivo.

E G Janzen, H J Stronks, C M Dubose, J L Poyer, P B McCay
PMCID: PMC1568620  PMID: 3007086

Abstract

The spin-trapping method is introduced and discussed. Some chemistry of nitroxides and nitrones is reviewed. Pattern recognition of ESR spectra of nitroxides is outlined. Factors controlling the magnitude of hyperfine splitting constants are mentioned. Methods of assigning spin adducts are listed. Review articles in the literature are referenced. Results in the electrochemical reduction of halocarbons are presented and some parallels with superoxide chemistry shown. Various speculative reactions are given. The in vitro and in vivo experiments where halocarbon radicals have been detected by spin trapping are reviewed and some new results reported. A comparison for different animals is added.

Full text

PDF
151

Selected References

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

  1. Ahr H. J., King L. J., Nastainczyk W., Ullrich V. The mechanism of reductive dehalogenation of halothane by liver cytochrome P450. Biochem Pharmacol. 1982 Feb 1;31(3):383–390. doi: 10.1016/0006-2952(82)90186-1. [DOI] [PubMed] [Google Scholar]
  2. Albano E., Lott K. A., Slater T. F., Stier A., Symons M. C., Tomasi A. Spin-trapping studies on the free-radical products formed by metabolic activation of carbon tetrachloride in rat liver microsomal fractions isolated hepatocytes and in vivo in the rat. Biochem J. 1982 May 15;204(2):593–603. doi: 10.1042/bj2040593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baker M. T., Van Dyke R. A. Metabolism-dependent binding of the chlorinated insecticide DDT and its metabolite, DDD, to microsomal protein and lipids. Biochem Pharmacol. 1984 Jan 15;33(2):255–260. doi: 10.1016/0006-2952(84)90483-0. [DOI] [PubMed] [Google Scholar]
  4. Carney F. M., Van Dyke R. A. Halothane hepatitis: a critical review. Anesth Analg. 1972 Jan-Feb;51(1):135–160. [PubMed] [Google Scholar]
  5. Castro C. E., Bartnicki E. W. Conformational isomerism and effective redox geometry in the oxidation of heme proteins by alkyl halides, cytochrome c, and cytochrome oxidase. Biochemistry. 1975 Feb 11;14(3):498–503. doi: 10.1021/bi00674a006. [DOI] [PubMed] [Google Scholar]
  6. Castro C. E. Theory of hemeprotein reactivity. J Theor Biol. 1971 Dec;33(3):475–490. doi: 10.1016/0022-5193(71)90092-0. [DOI] [PubMed] [Google Scholar]
  7. Finkelstein E., Rosen G. M., Rauckman E. J. Spin trapping of superoxide and hydroxyl radical: practical aspects. Arch Biochem Biophys. 1980 Mar;200(1):1–16. doi: 10.1016/0003-9861(80)90323-9. [DOI] [PubMed] [Google Scholar]
  8. Forni L. G., Packer J. E., Slater T. F., Willson R. L. Reaction of the trichloromethyl and halothane-derived peroxy radicals with unsaturated fatty acids: a pulse radiolysis study. Chem Biol Interact. 1983 Jul 15;45(2):171–177. doi: 10.1016/0009-2797(83)90066-2. [DOI] [PubMed] [Google Scholar]
  9. Fowler J. S. Chlorinated hydrocarbon toxicity in the fowl and duck. J Comp Pathol. 1970 Jul;80(3):465–471. doi: 10.1016/0021-9975(70)90079-4. [DOI] [PubMed] [Google Scholar]
  10. Fujii K., Miki N., Kanashiro M., Miura R., Sugiyama T., Morio M., Yamano T., Miyake Y. A spin trap study on anaerobic dehalogenation of halothane by a reconstituted liver microsomal cytochrome P-450 enzyme system. J Biochem. 1982 Jan;91(1):415–418. doi: 10.1093/oxfordjournals.jbchem.a133704. [DOI] [PubMed] [Google Scholar]
  11. Fujii K., Morio M., Kikuchi H., Ishihara S., Okida M., Ficor F. In vivo spin-trap study on anaerobic dehalogenation of halothane. Life Sci. 1984 Jul 30;35(5):463–468. doi: 10.1016/0024-3205(84)90238-8. [DOI] [PubMed] [Google Scholar]
  12. Hanzlik R. P. Reactivity and toxicity among halogenated methanes and related compounds. A physicochemical correlate with predictive value. Biochem Pharmacol. 1981 Nov 15;30(22):3027–3030. doi: 10.1016/0006-2952(81)90488-3. [DOI] [PubMed] [Google Scholar]
  13. Harbour J. R., Bolton J. R. Superoxide formation in spinach chloroplasts: electron spin resonance detection by spin trapping. Biochem Biophys Res Commun. 1975 Jan 2;64(3):803–807. doi: 10.1016/0006-291x(75)90118-7. [DOI] [PubMed] [Google Scholar]
  14. Janzen E. G. Spin trapping. Methods Enzymol. 1984;105:188–198. doi: 10.1016/s0076-6879(84)05025-4. [DOI] [PubMed] [Google Scholar]
  15. Kalyanaraman B., Mason R. P., Perez-Reyes E., Chignell C. F., Wolf C. R., Philpot R. M. Characterization of the free radical formed in aerobic microsomal incubations containing carbon tetrachloride and NADPH. Biochem Biophys Res Commun. 1979 Aug 28;89(4):1065–1072. doi: 10.1016/0006-291x(79)92116-8. [DOI] [PubMed] [Google Scholar]
  16. Lai C. S., Piette L. H. Spin-trapping studies of hydroxyl radical production involved in lipid peroxidation. Arch Biochem Biophys. 1978 Sep;190(1):27–38. doi: 10.1016/0003-9861(78)90250-3. [DOI] [PubMed] [Google Scholar]
  17. Lai E. K., McCay P. B., Noguchi T., Fong K. L. In vivo spin-trapping of trichloromethyl radicals formed from CCl4. Biochem Pharmacol. 1979 Jul 15;28(14):2231–2235. doi: 10.1016/0006-2952(79)90212-0. [DOI] [PubMed] [Google Scholar]
  18. McCay P. B., Lai E. K., Poyer J. L., DuBose C. M., Janzen E. G. Oxygen- and carbon-centered free radical formation during carbon tetrachloride metabolism. Observation of lipid radicals in vivo and in vitro. J Biol Chem. 1984 Feb 25;259(4):2135–2143. [PubMed] [Google Scholar]
  19. Nachtomi E. Effect of ethylene dibromide and carbon tetrachloride on lipid peroxidation in rat and chick liver. Exp Mol Pathol. 1972 Oct;17(2):171–175. doi: 10.1016/0014-4800(72)90066-4. [DOI] [PubMed] [Google Scholar]
  20. Noguchi T., Fong K. L., Lai E. K., Alexander S. S., King M. M., Olson L., Poyer J. L., McCay P. B. Specificity of a phenobarbital-induced cytochrome P-450 for metabolism of carbon tetrachloride to the trichloromethyl radical. Biochem Pharmacol. 1982 Mar 1;31(5):615–624. doi: 10.1016/0006-2952(82)90440-3. [DOI] [PubMed] [Google Scholar]
  21. Noguchi T., Fong K. L., Lai E. K., Olson L., McCay P. B. Selective early loss of polypeptides in liver microsomes of CCl4-treated rats. Relationship to cytochrome P-450 content. Biochem Pharmacol. 1982 Mar 1;31(5):609–614. doi: 10.1016/0006-2952(82)90439-7. [DOI] [PubMed] [Google Scholar]
  22. Plummer J. L., Beckwith A. L., Bastin F. N., Adams J. F., Cousins M. J., Hall P. Free radical formation in vivo and hepatotoxicity due to anesthesia with halothane. Anesthesiology. 1982 Sep;57(3):160–166. doi: 10.1097/00000542-198209000-00003. [DOI] [PubMed] [Google Scholar]
  23. Poyer J. L., Floyd R. A., McCay P. B., Janzen E. G., Davis E. R. Spin-trapping of the trichloromethyl radical produced during enzymic NADPH oxidation in the presence of carbon tetrachloride or bromotrichloromethane. Biochim Biophys Acta. 1978 Mar 20;539(3):402–409. doi: 10.1016/0304-4165(78)90044-2. [DOI] [PubMed] [Google Scholar]
  24. Poyer J. L., McCay P. B., Lai E. K., Janzen E. G., Davis E. R. Confirmation of assignment of the trichloromethyl radical spin adduct detected by spin trapping during 13C-carbon tetrachloride metabolism in vitro and in vivo. Biochem Biophys Res Commun. 1980 Jun 30;94(4):1154–1160. doi: 10.1016/0006-291x(80)90540-9. [DOI] [PubMed] [Google Scholar]
  25. Poyer J. L., McCay P. B., Weddle C. C., Downs P. E. In vivo spin-trapping of radicals formed during halothane metabolism. Biochem Pharmacol. 1981 Jun 15;30(12):1517–1519. doi: 10.1016/0006-2952(81)90375-0. [DOI] [PubMed] [Google Scholar]
  26. Rosen G. M., Kloss M. W., Rauckman E. J. Initiation of in vitro lipid peroxidation by N-hydroxynorcocaine and norcocaine nitroxide. Mol Pharmacol. 1982 Nov;22(3):529–531. [PubMed] [Google Scholar]
  27. Saprin A. N., Piette L. H. Spin trapping and its application in the study of lipid peroxidation and free radical production with liver microsomes. Arch Biochem Biophys. 1977 Apr 30;180(2):480–492. doi: 10.1016/0003-9861(77)90063-7. [DOI] [PubMed] [Google Scholar]
  28. Testa B., Jenner P. Inhibitors of Cytochrome P-450s and their mechanism of action. Drug Metab Rev. 1981;12(1):1–117. doi: 10.3109/03602538109011082. [DOI] [PubMed] [Google Scholar]
  29. Thompson J. A., Ho B., Mastovich S. L. Reductive metabolism of 1,1,1,2-tetrachloroethane and related chloroethanes by rat liver microsomes. Chem Biol Interact. 1984 Oct;51(3):321–333. doi: 10.1016/0009-2797(84)90157-1. [DOI] [PubMed] [Google Scholar]
  30. Tomasi A., Albano E., Lott K. A., Slater T. F. Spin trapping of free radical products of CC14 activation using pulse radiolysis and high energy radiation procedures. FEBS Lett. 1980 Dec 29;122(2):303–306. doi: 10.1016/0014-5793(80)80461-3. [DOI] [PubMed] [Google Scholar]
  31. Tomasi A., Billing S., Garner A., Slater T. F., Albano E. The metabolism of halothane by hepatocytes: a comparison between free radical spin trapping and lipid peroxidation in relation to cell damage. Chem Biol Interact. 1983 Sep 15;46(3):353–368. doi: 10.1016/0009-2797(83)90019-4. [DOI] [PubMed] [Google Scholar]
  32. Trudell J. R., Bösterling, Trevor A. 1-Chloro-2,2,2-trifluoroethyl radical: Formation from halothane by human cytochrome P-450 in reconstituted vesicles and binding to phospholipids. Biochem Biophys Res Commun. 1981 Sep 16;102(1):372–377. doi: 10.1016/0006-291x(81)91531-x. [DOI] [PubMed] [Google Scholar]
  33. West S. B., Huang M. T., Miwa G. T., Lu A. Y. A simple and rapid procedure for the purification of phenobarbital-inducible cytochrome P-450 from rat liver microsomes. Arch Biochem Biophys. 1979 Mar;193(1):42–50. doi: 10.1016/0003-9861(79)90006-7. [DOI] [PubMed] [Google Scholar]
  34. Wolf C. R., Mansuy D., Nastainczyk W., Deutschmann G., Ullrich V. The reduction of polyhalogenated methanes by liver microsomal cytochrome P450. Mol Pharmacol. 1977 Jul;13(4):698–705. [PubMed] [Google Scholar]
  35. de Groot H., Noll T. The crucial role of hypoxia in halothane-induced lipid peroxidation. Biochem Biophys Res Commun. 1984 Feb 29;119(1):139–143. doi: 10.1016/0006-291x(84)91629-2. [DOI] [PubMed] [Google Scholar]

Articles from Environmental Health Perspectives are provided here courtesy of National Institute of Environmental Health Sciences

RESOURCES