Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1977 Dec 15;168(3):417–422. doi: 10.1042/bj1680417

Loss of haem from cytochrome P-450 caused by lipid peroxidation and 2-allyl-2-isoprophylacetamide. An abnormal pathway not involving production of carbon monoxide.

F De Matteis, A H Gibbs, A Unseld
PMCID: PMC1183788  PMID: 606245

Abstract

1. Microsomal preparations undergoing lipid peroxidation produce CO and lose haem from cytochrome P-450. 2. The amount of CO produced does not correlate with the amount of haem lost and, after pre-labelling of microsomal haem in its bridges with 5-amino[5-14C]laevulinate, the radioactivity lost from haem is not recorved as CO. 3. Similarly, when pre-labelled microsomal haem is destroyed by the action of 2-allyl-2-isopropylacetamide, no radioactivity is recovered as CO. In clear contrast, on degradation of haem by the haem oxygenase system, CO is produced in an amount equimolar to the haem lost. 4. It is concluded that (a) the CO produced during lipid peroxidation originates from a source different from haem and (b) the degradations of haem caused by lipid peroxidation and 2-allyl-2-isopropylacetamide do not involve to any significant extent evolution of the methene-bridge carbon of haem as CO.

Full text

PDF
417

Selected References

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

  1. Aust S. D., Roerig D. L., Pederson T. C. Evidence for superoxide generation by NADPH-cytochrome c reductase of rat liver microsomes. Biochem Biophys Res Commun. 1972 Jun 9;47(5):1133–1137. doi: 10.1016/0006-291x(72)90952-7. [DOI] [PubMed] [Google Scholar]
  2. Beauchamp C., Fridovich I. A mechanism for the production of ethylene from methional. The generation of the hydroxyl radical by xanthine oxidase. J Biol Chem. 1970 Sep 25;245(18):4641–4646. [PubMed] [Google Scholar]
  3. Brown S. B., King R. F. 180 studies of haem catabolism. Biochem Soc Trans. 1976;4(2):197–201. doi: 10.1042/bst0040197. [DOI] [PubMed] [Google Scholar]
  4. COBURN R. F., DANIELSON G. K., BLAKEMORE W. S., FORSTER R. E., 2nd CARBON MONOXIDE IN BLOOD: ANALYTICAL METHOD AND SOURCES OF ERROR. J Appl Physiol. 1964 May;19:510–515. doi: 10.1152/jappl.1964.19.3.510. [DOI] [PubMed] [Google Scholar]
  5. DRESEL E. I., FALK J. E. Studies on the biosynthesis of blood pigments. I. Haem synthesis in haemolysed erythrocytes of chicken blood. Biochem J. 1954 Jan;56(1):156–163. doi: 10.1042/bj0560156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. De Matteis F. Loss of haem in rat liver caused by the porphyrogenic agent 2-allyl-2-isopropylacetamide. Biochem J. 1971 Oct;124(4):767–777. doi: 10.1042/bj1240767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. De Matteis F., Sparks R. G. Iron-dependent loss of liver cytochrome P-450 haem in vivo and in vitro. FEBS Lett. 1973 Jan 15;29(2):141–144. doi: 10.1016/0014-5793(73)80545-9. [DOI] [PubMed] [Google Scholar]
  8. De Matteis F., Unseld A. Increased liver haem degradation caused by foreign chemicals: a comparison of the effects of 2-allyl-2-isopropylacetamide and cobaltous chloride. Biochem Soc Trans. 1976;4(2):205–209. doi: 10.1042/bst0040205. [DOI] [PubMed] [Google Scholar]
  9. LABBE R. F., NISHIDA G. A new method of hemin isolation. Biochim Biophys Acta. 1957 Nov;26(2):437–437. doi: 10.1016/0006-3002(57)90033-1. [DOI] [PubMed] [Google Scholar]
  10. Landaw S. A., Callahan E. W., Jr, Schmid R. Catabolism of heme in vivo: comparison of the simultaneous production of bilirubin and carbon monoxide. J Clin Invest. 1970 May;49(5):914–925. doi: 10.1172/JCI106311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Landaw S. A., Winchell H. S. Endogenous production of carbon-14 labeled carbon monoxide: an in vivo technique for the study of heme catabolism. J Nucl Med. 1966 Sep;7(9):696–707. [PubMed] [Google Scholar]
  12. Levin W., Lu A. Y., Jacobson M., Kuntzman R., Poyer J. L., McCay P. B. Lipid peroxidation and the degradation of cytochrome P-450 heme. Arch Biochem Biophys. 1973 Oct;158(2):842–852. doi: 10.1016/0003-9861(73)90580-8. [DOI] [PubMed] [Google Scholar]
  13. Maines M. D., Kappas A. Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4293–4297. doi: 10.1073/pnas.71.11.4293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. McCord J. M., Fridovich I. The reduction of cytochrome c by milk xanthine oxidase. J Biol Chem. 1968 Nov 10;243(21):5753–5760. [PubMed] [Google Scholar]
  15. McDonagh A. F., Pospisil R., Meyer U. A. Degradation of hepatic haem to porphyrins and oxophlorins in rats treated with 2-allyl-2-isopropylacetamide. Biochem Soc Trans. 1976;4(2):297–298. doi: 10.1042/bst0040297. [DOI] [PubMed] [Google Scholar]
  16. OMURA T., SATO R. THE CARBON MONOXIDE-BINDING PIGMENT OF LIVER MICROSOMES. I. EVIDENCE FOR ITS HEMOPROTEIN NATURE. J Biol Chem. 1964 Jul;239:2370–2378. [PubMed] [Google Scholar]
  17. Poyer J. L., McCay P. B. Reduced triphosphopyridine nucleotide oxidase-catalyzed alterations of membrane phospholipids. IV. Dependence on Fe3+. J Biol Chem. 1971 Jan 10;246(1):263–269. [PubMed] [Google Scholar]
  18. Riely C. A., Cohen G., Lieberman M. Ethane evolution: a new index of lipid peroxidation. Science. 1974 Jan 18;183(4121):208–210. doi: 10.1126/science.183.4121.208. [DOI] [PubMed] [Google Scholar]
  19. Schacter B. A., Marver H. S., Meyer U. A. Heme and hemoprotein catabolism during stimulation of microsomal lipid peroxidation. Drug Metab Dispos. 1973 Jan-Feb;1(1):286–292. [PubMed] [Google Scholar]
  20. Sjöstrand T. Early studies of CO production. Ann N Y Acad Sci. 1970 Oct 5;174(1):5–10. doi: 10.1111/j.1749-6632.1970.tb49767.x. [DOI] [PubMed] [Google Scholar]
  21. Tenhunen R., Marver H. S., Schmid R. The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase. Proc Natl Acad Sci U S A. 1968 Oct;61(2):748–755. doi: 10.1073/pnas.61.2.748. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. WILBUR K. M., BERNHEIM F., SHAPIRO O. W. The thiobarbituric acid reagent as a test for the oxidation of unsaturated fatty acids by various agents. Arch Biochem. 1949 Dec;24(2):305–313. [PubMed] [Google Scholar]
  23. White P. Carbon monoxide production and heme catabolism. Ann N Y Acad Sci. 1970 Oct 5;174(1):23–31. doi: 10.1111/j.1749-6632.1970.tb49769.x. [DOI] [PubMed] [Google Scholar]
  24. Wills E. D. Lipid peroxide formation in microsomes. The role of non-haem iron. Biochem J. 1969 Jun;113(2):325–332. doi: 10.1042/bj1130325. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Wolff D. G. The formation of carbon monoxide during peroxidation of microsomal lipids. Biochem Biophys Res Commun. 1976 Dec 20;73(4):850–857. doi: 10.1016/0006-291x(76)90199-6. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES