3-Azidiamantane, a photolabile substrate analogue designed for photoaffinity labelling of phenobarbital-inducible cytochrome P-450

Biologia

Volumn 52, Issue 6, 1997, Pages 731-740

  Hodek, Petr ^a   Burkhard, Josef ^a  

^a CHARLES UNIVERSITY   (Czech Republic)

Author keywords

Cytochrome p 4500; I axidiamantane; Photoaffimty labelling; photolysis,

Indexed keywords

EID: 3042903924     PISSN: 00063088     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (42)

1. AXDERSSOX. L. A. & PETERSON. J. A. 1995. Activesite analysis of ferric P450 enzymes: hydrogenbonding effects on the circular dichroism spectra. Biorhem. Biophys. Res. Commun. 211: 389-395.
2. BAYLEY. H. 1983. Photogenerated reagents in biochemistry. WORK. T. S. & BURDON, R. H. (eds) 2nd ed. Eisevier Science, Amsterdam.
3. BAYLEY, H. & KNOWLES, J. R. 1978. Photogeneraed reagents for membrane labeling. 2. Phenvlcarbene and adarnantylidene formed within the lipid bilayer. Biochemistry 17: 2420-2423.
4. BRADLEY. C. F. EVANS, W. B. L. & STEVENS, I. D. R. 1977- Thermal and photochemical decomposition of cycloalkane spirodiazirines. J. Chern. Soc. Pcrkm Trans. 2: 1214-1220.
5. BURKHARD, .1. JANKü, J. VODICKA, L. & JEZIORSKI. .J. 1084. Diamantyl methanols; their oxidation by lead (IV) acetate. Sei. Papers Prague Inst. C'hem. Technol. D-49: 5-23.
6. OHOWDHRY. V. & WESTHEIMER. F. H. 1979. Photoamnity labeling of biological systems. Ann. Rev. Biochem. 48: 293-325.
7. COURTXEY. T. JOHNSTON, D. K. MCKERVEY. M. A. & ROONEY. .1. J. 1972. The chemistry of diamantane. Pari I. Synthesis and some functioiialisation reactions. J. ('hem. Soc. Perkin Trans. I: 2091- 2696.
8. DIONAM, .1. D. & STROBEL. 11. W. 1977. N'ADPHcytochroine P-450 reductase from rat liver: purification by affinity chromalography and characterization. Biochemistry 16: 1116 1123.
9. FLEMING. S. A. 1995. Chemical reagent s in photoaffinity labeling. Tetrahedron, 51: 12479 12520.
10. FRF.Y, A. H. KREIBICH. G. WADHERA. A. CI.ARKK. L. & WAXMAN. D. J. 198(i. 3-(Trifluoromethyl)-3-(m-125l]iodophenyl)diaziniie photolabels a substrate-binding site of rat hepatic cvtochrome P-150 form PB-4. Biochemistry 25: 4797 4803.
11. GuENGF.Rit'H. F. P. 1977. Separation and purification of multiple forms of iiiicrosomal cvtochrome P-450. Activities ol different forms of cvtochrome P-450 towards several compounds of environmental interest. J. Biol. ('hem. 252: 3970-3979.
12. GUENGERICH. F. P. 1988. Roles of cytorhromes P-450 in chemical carcinogenesis and cancer chemotherapy. Cancer Res. 48: 2946-2954.
13. HASEMANN, (A., RAVKTIANDRAN. K. G. PETERSON. .). A. .v- DEISENHOEER. .1. 1994. (Crystal structure and refinement of cytochrome P450ler]> at 2.3 A resolution. .1. Mol. Biol. 236: 1169 1185.
14. HAUGEN. L). A. & COON. M. .1. 197(i. Properties of elect rophoretically homogeneous phenobarbitalinducible and ,-uaplitlioflavone-inducible forms of liver microsomal cytochrome P-450. .J. Biol. Cliem. 251: 7929 7939.
15. HlLDKBRANDT, A. fi. LEIBMAX, K. C. A: ESTABROOK, R. iV. 1969. Metyrapone interact ion with hepatn microsomal cytochrome P-450 fron i rat s treated with phénobarbital. Biochem. Biophys. Res. Commun. 37: 477-485.
16. HODEK. P., BURKHARD, J. & JANKU, J. 1995. Probing the cytochrome P-450 2B1 active site with diamantoid compounds. Gen. Physiol. Biophys. 14: 225-239.
17. HODEK, P., JANSCäK, P., ANZENBACHER, P., BURKIARD. J., JANKü, J. & VODICKA, L. 1988. Metabolism of diamantane by rat liver microsomal cytochromes P-450. Xenobiotika 18: 1109-1118.
18. ISAEV, S. D. 1992. Personal communication.
19. ISAEV, S. D., KULIK, N. I. & YURCHENKO, A. G. 1993. Quantum-chemical study of adamantane-2-spirodiazirine protonation. Teor. Eksp. Khim. 29: 319325.
20. JANKü, J., BURKHARD, J. fe VODICKA, L. 1981. Hydrolyse von Bromderivaten des Diamantans mit Salpetersäure. Z. Chem. 21: 325-326.
21. JEFCOATE, C. R. 1978. Measurement of substrate and inhibitor binding to microsomal cytochrome P-450 by optical difference spectroscopy, pp. 258-279. In:
22. FLESCHER, S. fc PACKER, L. (eds) Methods in Enzymology Vol. 52, Academic Press, New York.
23. KAFKA, Z. & NâHûNEK, M. 1984. Triamantane: its synthesis and oxidation. Sei. Papers Prague Chem. Inst. Technol. D-55: 71-99.
24. LOWRY, O. H., ROSEBROUHG, N. J., FARR, A. L. & RANDALL, R. J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193: 265275.
25. MILLER. J. P. fc WHITE, R. E. 1994. Photoaffinity labeling of cytochrome P-450 2B4: Capture of active site heme ligands by a photocarbene. Biochemistry 33: 807-817.
26. NASH, T. 1953. The colorimetric estimation of formaldehyde by means of Hantsch reaction. J. Biochem. (Tokyo) 55: 416-421.
27. NEBERT. D. W. fe GONZALEZ, F. J. 1987. P450 genes: Structure, evolution, and regulation. Ann. Rev. Biochem. 56: 945-993.
28. NEGISHI, M., UNO, T., DARDEN, T. A., SUEYOSHI, T. & PEDERSEN, L. G. 1996. Structural flexibility and functional versatility of mammalian P450 enzymes. FASEB J. 10: 683-689.
29. NELSON. D. R., KOYMANS, L. KAMATAKI, T., STEGEMAN, J. J., FEYEREISEN, R., WAXMAN, D. J., WATERMAN, M. R. GOTOH, O., COON, M. J., Es-
30. TABROOK. R. W., GUNSALUS, I. C. fc NEBERT, D. W. 1996. P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics 6: 1-42.
31. OBACH, R. S., SPINK, D. C., CHEN, N. & KAMINSKY, L. S. 1992. Azidowarfarin photoaffinity probes of purified rat liver cytochrome P-4501A1. Arch. Biochem. Biophys. 294: 215-222.
32. OHNISHI, T., MIURA, S. & ICHIKAWA, Y. 1993. Photoaffinity labeling of cytochrome P-45011. Biochim. Biophys. Acta 1161: 257-264.
33. OMURA, T. & SATO, R. 1964. The carbon monoxidebinding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239: 2370-2378.
34. ORTIZ DE MONTELLANO, P. R. (ed), 1986. Cytochrome P-450: Structure, mechanism and biochemistry, Plenum Press, New York.
35. PORTER, T. D. fc COON, M. J. 1991. Cytochrome: Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms. J. Biol. Chem. 266: 13469-13472.
36. POULOS, T. L., FINZEL, B. C. fe HOWARD, A. J. 1987. High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195: 687-700.
37. RAVICHANDRAN, K. G., BODDUPALLI, S. S., HASEMANN, C. A., PETERSON, J. A. & DEISENHOFER, J. 1993. Crystal structure of hemoprotein domain of P-450BM-3, a prototype for microsomal P-450's. Nature 261: 731-736.
38. ROBERTS, E. S., PERNECKY, S. J., ALWORTH, W. L. & HOLLENBERG, P. F. 1996. A role of threonine 302 in the mechanism-based inactivation of P450 2B4 by 2-ethynylnaphthalene. Arch. Biochem. Biophys. 331: 170-176.
39. SCHENKMAN, J. B., REMMER, H. fc ESTABROOK, R. W. 1967. Spectral studies of drug interaction with hepatic microsomal cytochrome. Mol. Pharmacol. 3: 113-123. SMITH, R. A. G. fc KNOWLES, J. R. 1975. Preparation and photolysis of 3-aryl-3H-diazirines. J. Chem. Soc. Perkin Trans. 2: 686-694. VODICKA, L., BURKHARD, J., ZACHAR, P., ISAEV.
40. S. D., SAICHENKO, S. I., YURCHENKO, A. G. JANKû, J. 1985. Sintez diamantan-3-spiro-3diazirina i nekotorye ego reaktsii. Zh. Org. Khim. 21: 2569-2574.
41. WERRINGLOER, J. 1978. Assay of formaldehyde generated during microsomal oxidation reactions, pp. 297-302. In: FLESCHER, S. & PACKER, L. (eds), Methods in Enzymology Vol. 52, Academic Press. New York.
42. WIERINGA, J. H., WYNBERG, H. fe STRATING, J. 1974. Germinal l,l'-biadamantyl group as a stabilizer of reactive functions. l.T-Biadamantyldiazomethane, l,l'-biadamantylmethyleneiminoxyl, and l,l'-biadamantylmethyleneiminyl. Tetrahedron, 30: 30533058.