Destruction of Heme and Hemoproteins Mediated by Liver Microsomal Reduced Nicotinamide Adenine Dinucleotide Phosphate-Cytochrome P-450 Reductase

Biochemistry

Volumn 17, Issue 17, 1978, Pages 3633-3639

  Guengerich, F Peter ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEME; HEMOPROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

ANIMAL EXPERIMENT; IN VITRO STUDY; LIVER; LIVER MICROSOME; RAT;

ANIMAL; CARBON MONOXIDE; CYTOCHROME P-450 ENZYME SYSTEM; CYTOCHROME REDUCTASES; HEME; HEMEPROTEINS; MALE; MICROSOMES, LIVER; NADP; OXIDATION-REDUCTION; RATS; SPECTROPHOTOMETRY; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0018095311     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00610a033     Document Type: Article

References (47)

1. Bonnett, R., and Stewart, J. C. M. (1975), J. Chem. Soc., Perkin Trans. 1, 224.
2. Coon, M. J., Haugen, D. A., Guengerich, F. P., Vermilion, J. L., and Dean, W. L. (1976), in The Structural Basis of Membrane Function, Hatefi, Y., and Djavadi-Ohaniance, L., Ed., Academic Press, New York, N.Y., p 409.
3. Cooper, D. Y., Schleyer, H., Rosenthal, O., Levin, W., Lu, A. Y. H., Kuntzman, R., and Cooney, A. H. (1977), Eur. J. Biochem. 74, 69.
4. DeMatteis, F. (1971), Biochem. J. 124, 767.
5. DeMatteis, F., Gibbs, A. H., and Unseld, A. (1977), Biochem. J. 168, 417.
6. Estabrook, R. W., Hildebrandt, A. G., Baron, J., Netter, K. J., and Leibman, K. (1971), Biochem. Biophys. Res. Commun. 42, 132.
7. Fischer, H., and Müller, A. (1937), Z. Physiol. Chem. 246, 43.
8. Guengerich, F. P. (1977a), J. Biol. Chem. 252, 3970.
9. Guengerich, F. P. (1977b), Mol. Pharmacol. 13, 911.
10. Guengerich, F. P., and Aust, S. D. (1977), Mol. Pharmacol. 13, 185.
11. Guengerich, F. P., Ballou, D. P., and Coon, M. J. (1975), Biochem. Biophys. Res. Commun. 70, 951.
12. Guengerich, F. P., and Broquist, H. P. (1973), Biochemistry 12, 4270.
13. Guengerich, F. P., and Strickland, T. W. (1977), Mol. Pharmacol. 13, 993.
14. Hupka, A. L., and Karler, R. (1973), J. Reticuloendothel. Soc.14, 225.
15. Imai, Y. (1976), J. Biochem. (Tokyo) 80, 267.
16. Koch, R. R., Glende, E. A., Jr., and Rechnagel, R. O. (1974), Biochem. Pharmacol. 23, 2907.
17. Krasny, H. C., and Holbrook, D. J., Jr. (1977), Mol. Pharmacol. 13, 759.
18. Laemmli, U. K. (1970), Nature (London) 227, 680.
19. Lemberg, R. (1956), Rev. Pure Appl. Chem. 6, 1.
20. Levin, W., Lu, A. Y. H., Jacobson, M., Kuntzman, R., Poyer, J. L., and McCay, P. B. (1973), Arch. Biochem. Biophys. 158, 842.
21. Lightner, D. (1978), in The Porphyrins, Dolphin, D., Ed., Academic Press, New York, N.Y. (in press).
22. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951), J. Biol. Chem. 193, 265.
23. Maines, M. D., and Anders, M. W. (1973), Drug Metab. Dispos. 1, 293.
24. Maines, M. D., and Kappas, A. (1975), J. Biol. Chem. 250, 4171.
25. Maines, M. D., and Kappas, A. (1977), Biochemistry 16, 419.
26. Masters, B. S. S., and Schacter, B. A. (1976), Ann. Clin. Res. 8, 18.
27. Mattocks, A. R., and White, I. N. H. (1970), Anal. Biochem. 38, 529.
28. Nakajima, H. (1963), J. Biol. Chem. 238, 3797.
29. Nishibayashi, H., Omura, T., Sato, R., and Estabrook, R. W. (1968), in Structure and Function of Cytochromes, Oku-nuki, K., Kamen, M. D., and Sekuzu, I., Ed., University Park Press, Baltimore, Md., p 658.
30. Nordblom, G. D., and Coon, M. J. (1977), Arch. Biochem. Biophys. 180, 343.
31. Nordblom, G. D., White, R. E., and Coon, M. J. (1976), Arch. Biochem. Biophys. 175, 524.
32. O'Carra, P., and Colleran, E. (1970), J. Chromatogr. 50, 458.
33. Omura, T., and Sato, R. (1964), J. Biol. Chem. 239, 2370.
34. Paine, A. J., and Legg, R. F. (1978), Biochem. Biophys. Res. Commun. 81, 672.
35. Schacter, B. A., Nelson, E. B., Marver, H. S., and Masters, B. S. S. (1972), J. Biol. Chem. 247, 3601.
36. Schwartz, S., Berg, M. H., Bossenmaier, I., and Dinsmore, H. (1960), Methods Biochem. Anal. 8, 221.
37. Snyder, S. H., and Hendley, E. D. (1971), Methods Enzymol. 17B, 741.
38. Spatz, L., and Strittmatter, P. (1971), Proc. Natl. Acad. Sci. U.S.A. 68, 1042.
39. Spatz, L., and Strittmatter, P. (1973), J. Biol. Chem. 248, 793.
40. Tenhunen, R., Marver, H. S., and Schmid, R. (1969), J. Biol. Chem. 244, 6388.
41. Tenhunen, R., Ross, M. E., Marver, H. S., and Schmid, R. (1970), Biochemistry 9, 298.
42. van der Hoeven, T. A., and Coon, M. J. (1974), J. Biol. Chem. 249, 6302.
43. Welton, A. F., and Aust, S. D. (1972), Biochem. Biophys. Res. Commun. 49, 661.
44. Welton, A. F., Pederson, T. C., Buege, J. A., and Aust, S. D. (1973), Biochem. Biophys. Res. Commun. 54, 161.
45. Yoshida, T., and Kikuchi, G. (1977), J. Biochem. (Tokyo) 81, 265.
46. Yoshida, T., Takahashi, S., and Kikuchi, G. (1974), J. Biochem. (Tokyo) 75, 1187.
47. Ziegler, D. M., and Mitchell, C. H. (1972), Arch. Biochem. Biophys. 150, 116.