Interactions between cytochrome P450 and cytochrome b5

Drug Metabolism Reviews

Volumn 31, Issue 2, 1999, Pages 351-364

  Schenkman, John B ^a   Jansson, Ingela ^a  

^a UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

Author keywords

Cytochrome b5; Electron transfer; P450 topology; Protein protein interaction

Indexed keywords

CYTOCHROME B5; CYTOCHROME B5 REDUCTASE; CYTOCHROME P450; CYTOCHROME P450 REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

BAY REGION BINDING SITE; CONFERENCE PAPER; DRUG METABOLISM; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; OXIDATION REDUCTION REACTION; OXYGENATION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION;

ANIMALS; CYTOCHROME P-450 ENZYME SYSTEM; CYTOCHROMES B5; ELECTRON TRANSPORT; HUMANS; OXIDATION-REDUCTION; PROTEIN CONFORMATION;

EID: 0032932418     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-100101923     Document Type: Conference Paper

References (79)

1. T. Shimakata, K. Mihara, and R. Sato, J. Biochem., 72, 1163 (1972).
2. S. R. Keyes, J. A. Alfano, I. Jansson, and D. L. Cinti, J. Biol. Chem., 254, 7778 (1979).
3. A. Hildebrandt and R. W. Estabrook, Arch. Biochem. Biophys., 143, 66 (1971).
4. A. Conney, R. R. Brown, J. A. Miller, and E. C. Miller, Cancer Res., 17, 628 (1957).
5. A. Nilsson and B. C. Johnson, Arch. Biochem. Biophys., 101, 494 (1963).
6. M. A. Correia and G. J. Mannering, Mol. Pharmacol., 9, 470 (1973).
7. H. A. Sasame, J. R. Mitchell, S. Thorgeirsson, and J. R. Gillette, Drug Metab. Dispos., 1, 150 (1973).
8. G. J. Mannering, S. Kuwahara, and T. Omura, Biochem. Biophys. Res. Commun., 57, 476 (1974).
9. I. Jansson and J. B. Schenkman, Arch. Biochem. Biophys., 178, 89 (1977).
10. M. Noshiro, N. Harada, and T. Omura, Biochem. Biophys. Res. Commun., 91, 207 (1979).
11. V. Ullrich, Z. Naturforsch., 24, 699 (1969).
12. M. R. Waterman and H. S. Mason, Arch. Biochem. Biophys., 150, 57 (1972).
13. J. A. Peterson, R. E. White, M. L. Coomes, D. H. O'Keeffe, R. E. Ebel, B. S. S. Masters, D. P. Ballou, and M. J. Coon, J. Biol. Chem., 252, 4431 (1977).
14. B. S. Cohen and R. W. Estabrook, Arch. Biochem. Biophys., 143, 54 (1971).
15. K. Netter and H. Illing, Xenobiotica, 4, 549 (1974).
16. I. Jansson and J. B. Schenkman, Arch. Biochem. Biophys., 185, 251 (1978).
17. I. Jansson and J. B. Schenkman, Mol. Pharmacol., 9, 840 (1973).
18. E. G. Hrycay and R. W. Estabrook, Biochem. Biophys. Res. Commun., 60, 771 (1974).
19. I. Jansson and J. B. Schenkman, Mol. Pharmacol., 11, 450 (1975).
20. J. B. Schenkman, A. I. Voznesensky, and I. Jansson, Arch. Biochem. Biophys., 314, 234 (1994).
21. C. Bonfils, C. Balny, and P. Maurel, J. Biol. Chem., 256, 9457 (1981).
22. D. Pompon and M. J. Coon, J. Biol. Chem., 259, 15377 (1984).
23. P. P. Tamburini, R. E. White, and J. B. Schenkman, J. Biol. Chem., 260, 4007 (1985).
24. M. Noshiro, V. Ullrich, and T. Omura, Eur. J. Biochem., 116, 521 (1981).
25. P. P. Tamburini and J. B. Schenkman, Proc. Natl. Acad. Sci. USA, 84, 11 (1987).
26. E. Canova-Davis, J. Y. L. Chiang, and L. A. Waskell, Biochem. Pharmacol., 34, 1907 (1985).
27. E. T. Morgan and M. J. Coon, Drug Metab. Dispos., 12, 358 (1984).
28. W. L. Backes and C. S. Eyer, J. Biol. Chem., 264, 6252 (1989).
29. T. Sugiyama, N. Miki, and T. Yamano, Biochem. Biophys. Res. Commun., 90, 715 (1979).
30. H. Yamazaki, M. Nakano, Y. Imai, Y.-F. Ueng, F. P. Guengerich, and T. Shimada, Arch. Biochem. Biophys., 325, 174 (1996).
31. I. Jansson, P. P. Tamburini, L. V. Favreau, and J. B. Schenkman, Drug Metab. Dispos., 13, 453 (1985).
32. J. Y. L. Chiang, Arch. Biochem. Biophys., 211, 662 (1981).
33. R. Juvonen, M. Iwasaki, and M. Negishi, Biochemistry, 31, 11519 (1992).
34. S. Kuwahara and T. Omura, Biochem. Biophys. Res. Commun., 96, 1562 (1980).
35. N. Miki, T. Sugiyama, T. Yamano, and Y. Miyake, Biochem. Int., 3, 217 (1981).
36. D. C. Eberhart and A. Parkinson. Arch. Biochem. Biophys., 291, 231 (1991).
37. M. S. Shet, K. M. Faulkner, P. L. Holmans, C. W. Fisher, and R. W. Estabrook, Arch. Biochem. Biophys., 318, 314 (1995).
38. H. Yamazaki, Y.-F. Ueng, T. Shimada, and F. P. Guengerich, Biochemistry, 34, 8380 (1995).
39. H. Yamazaki, W. W. Johnson, Y.-F. Ueng, T. Shimada, and F. P. Guengerich, J. Biol. Chem., 271, 27438 (1996).
40. J. D. Lipscomb, S. G. Sligar, M. J. Namtvedt, and I. C. Gunsalus, J. Biol. Chem., 251, 1116 (1976).
41. D. M. Davies and J. M. Lawther, Biochem. J., 258, 375 (1989).
42. F. Lederer, Biochimie, 76, 674 (1994).
43. S. Ng, M. B. Smith, H. T. Smith, and F. Millett, Biochemistry, 16, 4975 (1977).
44. F. S. Mathews, M. Levine, and P. Argos, J. Mol. Biol., 64, 449 (1972).
45. R. E. Dickerson, T. Takano, D. Eisenberg, O. B. Kallei, L. Samson, A. Cooper, and E. Margoliash, J. Biol. Chem., 246, 1511 (1971).
46. F. Salemme, J. Mol. Biol., 102, 563 (1976).
47. K. K. Rodgers, T. C. Pochapsky, and S. G. Sligar, Science, 240, 1657 (1988).
48. P. S. Stayton, T. L. Poulos, and S. G. Sligar, Biochemistry, 28, 8201 (1989).
49. A. Loverde and P. Strittmatter, J. Biol. Chem., 243, 5779 (1968).
50. H. A. Dailey and P. Strittmatter, J. Biol. Chem., 254, 5388 (1979).
51. H. A. Dailey and P. Strittmatter, J. Biol. Chem., 255, 5184 (1980).
52. J. D. Lambeth, L. M. Geren, and F. Millett, J. Biol. Chem., 259, 10025 (1984).
53. P. P. Tamburini and J. B. Schenkman, Arch. Biochem. Biophys., 245, 512 (1986).
54. P. S. Stayton, M. T. Fisher, and S. G. Sligar, J. Biol. Chem., 263, 13544 (1988).
55. A. I. Voznesensky and J. B. Schenkman, J. Biol. Chem., 269, 15724 (1994).
56. D. R. Nelson and H. W. Strobel, Biochemistry, 28, 656 (1989).
57. O. Gotoh and Y. Fujii-Kuriyama, in Frontiers in Biotransformation (K. Ruckpaul and H. Rein, eds.), Akademie-Verlag, Berlin, 1989, Vol. 1, p. 195.
58. C. A. Hasemann, R. G. Kurumbail, S. S. Boddupalli, J. A. Peterson, and J. Deisenhofer, Structure, 2, 41 (1995).
59. Y. T. Chang, O. B. Stiffelman, and G. H. Loew, Biochemie, 78, 771-779 (1996).
60. W. Pyerin, C. R. Wolf, V. Kinzel, D. Kubler, and F. Oesch, Carcinogenesis, 4, 573 (1983).
61. I. Jansson, P. M. Epstein, S. Bains, and J. B. Schenkman, Arch. Biochem. Biophys., 259, 441 (1987).
62. P. M. Epstein, M. Curti, I. Jansson, C.-K. Huang, and J. B. Schenkman, Arch. Biochem. Biophys., 271, 424 (1989).
63. R. Muller, W. Schmidt, and A. Stier, FEBS Lett., 187, 21 (1985).
64. P. S. Stayton and S. G. Sligar, Biochemistry, 29, 7381 (1990).
65. K. Nakamura, T. Horiuchi, T. Yasukochi, K. Sekimizu, T. Hara, and Y. Sagara, Biochim. Biophys. Acta, 1207, 40 (1994).
66. H. Koga, Y. Sagara, T. Yaoi, M. Tsujimura, K. Nakamura, K. Sekimizu, R. Makino, H. Shimada, Y. Ishimura, K. Yura, M. Go, M. Ikeguchi, and T. Horiuchi, FEBS Lett., 331, 109 (1993).
67. R. Lindberg, B. Burkart, T. Ichikawa, and M. Negishi, J. Biol. Chem., 264, 6465 (1989).
68. P. P. Tamburini and J. B. Schenkman, Mol. Pharmacol., 30, 178 (1986).
69. G. N. Chuev and V. D. Lakhno, J. Theoret. Biol., 163, 51 (1993).
70. T. L. Poulos and J. Kraut, J. Biol. Chem., 255, 10322 (1980).
71. D. N. Beratan, J. N. Onuchic, J. R. Winkler, and H. B. Gray, Science, 258, 1740 (1992).
72. M. D. Davies, L. Qin, J. L. Beck, K. S. Suslick, H. Koga, T. Horiuchi, and S. G. Sligar, J. Am. Chem. Soc., 112, 7396 (1990).
73. P. S. Stayton and S. G. Sligar, Biochemistry, 30, 1845 (1991).
74. J. E. Baldwin, G. M. Morris, and W. G. Richards, Proc. Roy. Soc. B, 245, 43 (1991).
75. T. L. Poulos, B. C. Finzel, and A. J. Howard, Biochemistry, 25, 5314 (1986).
76. J. T. Hazzard, G. McLendon, M. A. Cusanovich, and G. Tollin, Biochem. Biophys. Res. Commun., 151, 429 (1988).
77. B. M. Hoffman and M. A. Ratner, J. Am. Chem. Soc., 109, 6237 (1987).
78. Z. Zhang, A. Nassar, Z. Lu, J. B. Schenkman, and J. F. Rusling, J. Chem. Soc., Faraday Trans., 93, 1769 (1997).
79. E. Laviron, J. Electrochem. Chem., 101, 19 (1979).