Exceptionally stable salt bridges in cytochrome P450cam have functional roles

Biochemistry

Volumn 36, Issue 18, 1997, Pages 5402-5417

  Lounnas, Valère ^a   Wade, Rebecca C ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME P450;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

BINDING SITES; CAMPHOR; COMPUTER SIMULATION; CYTOCHROME P-450 ENZYME SYSTEM; ELECTROSTATICS; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MUTATION; OSMOLAR CONCENTRATION; OXYGENASES; PSEUDOMONAS PUTIDA; SALTS; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); DRYOBALANOPS; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0030917740     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9622940     Document Type: Article

References (54)

1. Anderson, D. E., Beckel, W. J., & Dahlquist, F. W. (1990) Biochemistry 29, 2403-2408.
2. Antosiewicz, J., McCammon, J. A., & Gilson, M. K. (1994) J. Mol. Biol. 238, 415-436.
3. Barlow, D. J., & Thornton, J. M. (1983) J. Mol. Biol. 168, 867-885.
4. Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) J. Comput. Chem. 4, 187-217.
5. Dao-pin, S., Nicholson, H., & Matthews, B. W. (1991) Biochemistry 30, 7142-7153.
6. Davis, M. E., & McCammon, J. A. (1989) J. Comput. Chem. 10, 386-391.
7. Davis, M. E., & McCammon, J. A. (1991) J. Comput. Chem. 12, 909-912.
8. Demchuk, E., & Wade, R. C. (1996) J. Phys. Chem. 100, 17373-17387.
9. Deprez, E., Gerber, N. C., Di Primo, C., Douzou, P., Sligar, S. G., & Hui Bon Hoa, G. (1994) Biochemistry 33, 14464-14468.
10. Di Primo, C., Deprez, E., Sligar, S. G., & Hui Bon Hoa, G. (1997) Biochemistry 36, 112-118.
11. FASEB (1992) FASEB J. 6, 667-792.
12. FASEB (1996) FASEB J. 10, 202-214.
13. Feher, V., Baldwin, E. P., & Dahlquist, F. W. (1996) Nat. Struct. Biol. 3, 516-521.
14. Fersht, A. R. (1972) J. Mol. Biol. 64, 497-509.
15. Gandini, D., Gogioso, L., Bolognesi, M., & Bordo, D. (1996) Proteins: Struct., Funct., Genet. 24, 439-449.
16. Gerber, N. C., & Sligar, S. G. (1992) J. Am. Chem. Soc. 114, 8742-8743.
17. Gerber, N. C., & Sligar, S. G. (1994) J. Biol. Chem. 269, 4260-4266.
18. Gilson, M. K., Sharp, K. A., & Honig, B. H. (1987) J. Comput. Chem. 9, 327-335.
19. Goodford, P. J. (1985) J. Med. Chem. 28, 849-857.
20. Griffin, B. W., & Peterson, J. A. (1972) Biochemistry 11, 4740-4746.
21. Hasemann, C. A., Ravichandran, K. G., Peterson, J. A., & Deisenhofer, J. (1994) J. Mol. Biol. 236, 1169-1185.
22. Hasemann, C. A., Kurumbail, R. G., Boddupalli, S., Peterson, J. A., & Deisenhofer, J. (1995) Structure 3, 41-62.
23. Helms, V., & Wade, R. C. (1995) Biophys. J. 69, 810-824.
24. Hendsch, Z. S., & Tidor, B. (1994) Protein Sci. 3, 211-226.
25. Hooft, R. W. W., Sander, C., & Vriend, G. (1996) Proteins: Struct., Funct., Genet. 26, 363-376.
26. Horowitz, A., Serrano, L., Avron, B., Bycroft, M., & Fersht, A. R. (1990) J. Mol. Biol. 216, 1031-1044.
27. Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., & Klein, M. L. (1983) J. Chem. Phys. 79, 926-935.
28. Koga, H., Sagara, Y., Yaoi, T., Tsujimara, M., Nakamura, K., Sekimizu, K., Nakino, R., Shimada, H., Ishimura, Y., Yura, K., Go, M., Ikeguchi, M., & Horiuchi, T. (1993) FEBS Lett. 331, 109-113.
29. Kuczera, K., Kuriyan, J., & Karplus, M. (1990) J. Mol. Biol. 213, 351-373.
30. Lee, B., & Richards, F. M. (1971) J. Mol. Biol. 55, 379-400.
31. Lumb, K. J., & Kim, P. S. (1995) Science 268, 436-439.
32. Lyu, P. C., Gansm P. J., & Kallenbach, N. R. (1992) J. Mol. Biol. 223, 343-350.
33. Madura, J. D., Davis, M. E., Gilson, M., Wade, R. C., Luty, B. A., & McCammon, J. A. (1994) Rev. Comput. Chem. 5, Chapt. 4.
34. Madura, J. D., Briggs, J. M., Wade, R. C., Davis, M. E., Luty, B. A., Ilin, A., Antosiewicz, J., Gilson, M. K., Bagheri, B., Scott, L. R., & McCammon, J. A. (1995) Comput. Phys. Commun. 91, 57-95.
35. Mohan, V., Davis, M. E., McCammon, J. A., & Pettitt, B. M. (1992) J. Phys. Chem. 96, 6328-6431.
36. Musafia, B., Burchner, V., & Arad, D. (1995) J. Mol. Biol. 254, 761-770.
37. Perutz, M. (1978) Science 201, 1187-1191.
38. Pfeil, W., Noelting, B. O., & Jung, C. (1993) Biochemistry 32, 8856-8862.
39. Poulos, T. L. (1995) Curr. Opin. Struct. Biol. 6, 767-774.
40. Poulos, T. L., & Raag, R. (1992) FASEB J. 6, 674-679.
41. Poulos, T. L., Finzel, B. C., & Howard, A. J. (1986) Biochemistry 25, 5314-5322.
42. Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) J. Mol. Biol. 195, 687-700.
43. Ravichandran, K. G., Boddupalli, S. S., Hasemann, C. A., Peterson, J. A., & Deisenhofer, J. (1993) Science 261, 731-736.
44. Richards, F. M. (1979) Carlsberg Res. Commun. 44, 47-63.
45. Ryckaert, J.-P., Cicotti, G., & Berendsen, H. J. C. (1977) J. Comput. Phys. 23, 327-341.
46. Schueler, O., & Margalit, H. (1995) J. Mol. Biol. 248, 125-135.
47. Shoichet, B. K., Baasee, W. A., Kuroki, R., & Matthews, B. W. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 452-456.
48. Sligar, S. G. (1976) Biochemistry 24, 5399-5406.
49. Straatsma, T. P., & McCammon, J. A. (1990) J. Comput. Chem. 11, 943-951.
50. Vriend, G. (1990) J. Mol. Graph. 8, 52-56.
51. Waldburger, C. D., Schilbach, J. E., & Sauer, R. T. (1995) Struct. Biol. 2, 122-128.
52. Warshel, A., & Russel, S. T. (1984) Q. Rev. Biophys. 17, 283-422.
53. Wimley, W. C., Gawrisch, K., Creamer, T. P., & White, S. H. (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 2985-2990.
54. Yip, K. S. P., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnivoka, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R., Consalvi, V., Scandurra, R., & Rice, D. W. (1995) Structure 3, 1147-1158.