Influence of mutation of the amino-terminal signal anchor sequence of cytochrome P450 2B4 on the enzyme structure and electron transfer processes

Journal of Biochemistry

Volumn 124, Issue 2, 1998, Pages 396-403

  Lehnerer, Michael ^a   Schulze, Johannes ^a   Pernecky, Steven J ^b   Lewis, David F V ^c   Eulitz, Manfred ^d   Hlavica, Peter ^a  

^a UNIVERSITY OF MUNICH   (Germany)

^b EASTERN MICHIGAN UNIVERSITY   (United States)

^c UNIVERSITY OF SURREY   (United Kingdom)

^d INSTITUTE OF EPIDEMIOLOGY   (Germany)

Author keywords

Cytochrome P450 2B4; Electron transfer processes; NH2 terminus; Site directed mutagenesis

Indexed keywords

CYTOCHROME B5; CYTOCHROME P450; HEMOPROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SIGNAL PEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVITY; MICHAELIS MENTEN KINETICS; MUTATION; NONHUMAN;

EID: 0031711047     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022125     Document Type: Article

References (44)

1. Porter, T.D. and Coon, M.J. (1991) Cytochrome P450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms. J. Biol. Chem. 266, 13469-13472
2. Lu, A.Y.H. and Coon, M.J. (1968) Role of hemoprotein P-450 in fatty acid ω-hydroxylation in a soluble enzyme system from liver microsomes. J. Biol. Chem. 243, 1331-1332
3. 5. Drug Metab. Dispos. 12, 358-364
4. Tamburini, P.P. and Schenkman, J.B. (1986) Differences in the mechanism of functional interaction between NADPH-cytochrome P-450 reductase and its redox partners. Mol. Pharmacol. 30, 178-185
5. 5. J. Biol. Chem. 260, 4007-4015
6. 5. Biochem. J. 318, 857-862
7. Bernhardt, R., Kraft, R., Otto, A., and Ruckpaul, K. (1988) Electrostatic interactions between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase. Biomed. Biochim. Acta 47, 581-592
8. Shen, S. and Strobel, H.W. (1992) The role of cytochrome P450 lysine residues in the interaction between cytochrome P450IA1 and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 294, 83-90
9. Voznesensky, A.I. and Schenkman, J.B. (1992) The cytochrome P450 2B4-NADPH cytochrome P450 reductase electron transfer complex is not formed by charge-pairing. J. Biol. Chem. 267, 14669-14676
10. Haugen, D.A., Armes, L.G., Yasunobu, K.T., and Coon, M.J. (1977) Amino-terminal sequence of phenobarbital-inducible cytochrome P-450 from rabbit liver microsomes: similarity to hydrophobic amino-terminal segments of preproteins. Biochem. Biophys. Res. Commun. 77, 967-973
11. Dong, M.S., Yamazaki, H., Guo, Z., and Guengerich, F.P. (1996) Recombinant human cytochrome P450 1A2 and an N-terminal-truncated form: construction, purification, aggregation properties, and interactions with flavodoxin, ferredoxin, and NADPH-cytochrome P450 reductase. Arch. Biochem. Biophys. 327, 11-19
12. 2-terminal region and expressed in Escherichia coli. Arch. Biochem. Biophys. 318, 446-456
13. Li, Y.C. and Chiang, J.Y. (1991) The expression of a catalytically active cholesterol 7α-hydroxylase cytochrome P450 in Escherichia coli. J. Biol. Chem. 266, 19186-19191
14. Scheller, U., Kraft, R., Schröder, K.L., and Schunck, W.H. (1994) Generation of the soluble and functional cytosolic domain of microsomal cytochrome P450 52A3. J. Biol. Chem. 269, 12779-12783
15. Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 239, 2379-2385
16. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
17. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354
18. Hlavica, P. and Hülsmann, S. (1979) Studies of the mechanism of hepatic microsomal N-oxide formation. N-oxidation of N,N-dimethylaniline by a reconstituted rabbit liver microsomal cytochrome P-448 enzyme system. Biochem. J. 182, 109-116
19. 5. Methods Enzymol. 52, 97-101
20. 5 reductase. Methods Enzymol. 52, 102-108
21. Tamburini, P.P. and Schenkman, J.B. (1987) Purification to homogeneity and enzymological characterization of a functional covalent complex composed of cytochromes P-450 isozyme 2 and ba from rabbit liver. Proc. Natl. Acad. Sci. USA 84, 11-15
22. French, J.S., Guengerich, F.P., and Coon, M.J. (1980) Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system. J. Biol. Chem. 255, 4112-4119
23. Ragone, R., Colonna, G., Balestrieri, C., Servillo, L., and Irace, G. (1984) Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 23, 1871-1875
24. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275
25. Greenfield, N. and Fasman, G.D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116
26. Lewis, D.F.V. and Lake, B.G. (1997) Molecular modelling of mammalian CYP2B isoforms and their interaction with substrates, inhibitors and redox partners. Xenobiotica 27, 443-478
27. Haugen, D.A. and Coon, M.J. (1976) Properties of electrophoretically homogenous phenobarbital-inducible and β-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J. Biol. Chem. 251, 7929-7939
28. Schwarze, W., Bernhardt, R., Jänig, G.R., and Ruckpaul, K. (1983) Fluorescent energy transfer measurements on fluorescein isothiocyanate modified cytochrome P-450 LM2. Biochem. Biophys. Res. Commun. 113, 353-360
29. Tarr, G.E., Black, S.D., Fujita, V.S., and Coon, M.J. (1983) Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes. Proc. Natl. Acad. Sci. USA 80, 6552-6556
30. Inouye, K. and Coon, M.J. (1985) Properties of the tryptophan residues in rabbit liver microsomal cytochrome P-450 isozyme 2 as determined by fluorescence. Biochem. Biophys. Res. Commun. 128, 676-682
31. Ross, J.B.A., Szabo, A.G., and Hogue, C.W.V. (1997) Enhancement of protein spectra with tryptophan analogs: fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions. Methods Enzymol. 278, 151-190
32. Finazzi-Agro, A., Rotilio, G., Avigliano, L., Guerrieri, P., Boffi, V., and Mondovi, B. (1970) Environment of copper in Pseudomonas fluorescens azurin: fluorimetric approach. Biochemisry 9, 2009-2014
33. Schulz, G.E. and Schirmer, R.H. (1978) Principles of Protein Structure, p. 30, Springer-Verlag, Berlin
34. Tretiakov, V.E., Degtyarenko, K.N., Uvarov, V.Y., and Archakov, A.I. (1989) Secondary structure and membrane topology of cytochrome P450s. Arch. Biochem. Biophys. 275, 429-439
35. Chen, C.D., Doray, B., and Kemper, B. (1997) Efficient assembly of functional cytochrome P450 2C2 requires a spacer sequence between the N-terminal signal anchor and catalytic domains. J. Biol. Chem. 272, 22891-22897
36. Davydov, D.R., Knyushko, T.V., Kanaeva, I.P., Koen, Y.M., Samenkova, N.F., Archakov, A.I., and Hui Bon Hoa, G. (1996) Interactions of cytochrome P450 2B4 with NADPH-cytochrome P450 reductase studied by fluorescent probe. Biochimie 78, 734-743
37. 5 and NADPH-flavoprotein in complex formation. Biochem. Mol. Biol. Int. 42, 731-737
38. Nordblom, G.D. and Coon, M.J. (1977) Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450. Arch. Biochem. Biophys. 180, 343-347
39. Vaz, A.D.N., Pernecky, S.J., Raner, G.M., and Coon, M.J. (1996) Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reactions: switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4. Proc. Natl. Acad. Sci. USA 93, 4644-4648
40. 5-enriched rabbit liver microsomal fractions. Biochim. Biophys. Acta 913, 219-227
41. Hrycay, E.G., Gustafsson, J.A., Ingelman-Sundberg, M., and Ernster, L. (1976) The involvement of cytochrome P-450 in hepatic microsomal steroid hydroxylation reactions supported by sodium periodate, sodium chlorite, and organic hydroperoxides. Eur. J. Biochem. 61, 43-52
42. Ruf, H.H. and Eichinger, V. (1982) Microsomal electron transport. The rate of the electron transfer to oxygenated cytochrome P450 in Cytochrome P450, Biochemistry, Biophysics and Environmental Implications (Hietanen, E., Laitinen, M., and Hänninen, O., eds.) pp. 597-600, Elsevier Biomedical Press, Amsterdam
43. Gillam, E.M.J., Baba, T., Kim, B.R., Ohmori, S., and Guengerich, F.P. (1993) Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 305, 123-131
44. 2-terminal membrane-insertion signal peptide does not alter the catalytic activities. Proc. Natl. Acad. Sci. USA 88, 9141-9145