Engineering cytochrome c peroxidase into cytochrome P450: A proximal effect on heme-thiolate ligation

Biochemistry

Volumn 38, Issue 34, 1999, Pages 11122-11129

  Sigman, Jeffrey A ^a   Pond, Alycen E ^b   Dawson, John H ^b,c   Lu, Yi ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF SOUTH CAROLINA   (United States)

^c UNIVERSITY OF SOUTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CYSTEIC ACID; CYSTEINE; CYTOCHROME C PEROXIDASE; CYTOCHROME P450; FERRICYANIDE; HEMOPROTEIN; IMIDAZOLE; LEUCINE; MUTANT PROTEIN; THIOL DERIVATIVE;

ABSORPTION SPECTROSCOPY; ARTICLE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME MODIFICATION; ENZYME STRUCTURE; LIGAND BINDING; NONHUMAN; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ASPARTIC ACID; CIRCULAR DICHROISM; CYSTEINE; CYTOCHROME C GROUP; CYTOCHROME P-450 ENZYME SYSTEM; CYTOCHROME-C PEROXIDASE; CYTOCHROMES C; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; FERRIC COMPOUNDS; HEME; HISTIDINE; IMIDAZOLES; LEUCINE; LIGANDS; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; SPECTROPHOTOMETRY, ULTRAVIOLET;

EID: 0033600588     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990815o     Document Type: Article

References (64)

1. Bertini, I., Gray, H. B., Lippard, S. J., and Valentine, J. S. (1994) Bioinorganic Chemistry, University Science Books, Sausalito, CA.
2. Sono, M., Roach, M. P., Coulter, E. D., and Dawson, J. H. (1996) Chem. Rev. 96, 2841-2887.
3. Erman, J. E., Hager, L. P., and Sligar, S. G. (1994) Adv. Inorg. Biochem. 70, 71-118.
4. Sono, M., Stuehr, D. J., Ikada-Saito, M., and Dawson, J. H. (1995) J. Biol. Chem. 270, 19943-19948.
5. Shelver, D., Thorsteinsson, M. V., Kerby, R. L., Chung, S. Y., Roberts, G. P., Reynolds, M. F., Parks, R. B., and Burstyn, J. N. (1999) Biochemistry 38, 2669-2678.
6. Sligar, S. G., Egeberg, K. D., Sage, J. T., Morikis, D., and Champion, P. M. (1987) J. Am. Chem. Soc. 109, 7896-7897.
7. Barker, P. D., Nerou, E. P., Cheesman, M. R., Thomson, A. J., de Oliveira, P., and Hill, H. A. O. (1996) Biochemistry 35, 13618-13626.
8. Raphael, A. L., and Gray, H. B. (1991) J. Am. Chem. Soc. 113, 1038-1040.
9. Adachi, S.-i., Nagano, S., Watanabe, Y., Ishimori, K., and Morishima, I. (1991) Biochem. Biophys. Res. Commun. 180, 138-144.
10. Adachi, S.-i., Nagano, S., Ishimori, K., Watanabe, Y., Morishima, I., Egawa, T., Kitagawa, T., and Makino, R. (1993) Biochemistry 32, 241-252.
11. Hildebrand, D. P., Ferrer, J. C., Tang, H.-L., Smith, M., and Mauk, A. G. (1995) Biochemistry 34, 11598-11605.
12. Hildebrand, D. P., Burk, D. L., Maurus, R., Ferrer, J. C., Brayer, G. D., and Mauk, A. G. (1995) Biochemistry 34, 1997-2005.
13. Matsui, T., Nagano, S., Ishimori, K., Watanabe, Y., and Morishima, I. (1996) Biochemistry 35, 13118-13124.
14. Choudhury, K., Sundaramoorthy, M., Mauro, J. M., and Poulos, T. L. (1992) J. Biol. Chem. 267, 25656-25659.
15. Choudhury, K., Sundaramoorthy, M., Hickman, A., Yonetani, T., Woehl, E., Dunn, M. F., and Poulos, T. L. (1994) J. Biol. Chem. 269, 20239-20249.
16. Smulevich, G., Neri, F., Willemsen, O., Choudhury, K., Marzocchi, M. P., and Poulos, T. L. (1995) Biochemistry 34, 13485-13490.
17. Lu, Y., Casimiro, D. R., Bren, K. L., Richards, J. H., and Gray, H. B. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 11456-11459.
18. DePillis, G. D., Decatur, S. M., Barrick, D., and Boxer, S. G. (1994) J. Am. Chem. Soc. 116, 6981-6982.
19. Barrick, D. (1994) Biochemistry 33, 6546-6554.
20. McRee, D. E., Jensen, G. M., Fitzgerald, M. M., Siegel, H. A., and Goodin, D. B. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 12847-12851.
21. Wilks, A., Sun, J., Loehr, T. M., and Ortiz de Montellano, P. R. (1995) J. Am. Chem. Soc. 117, 2925-2926.
22. Newmyer, S. L., Sun, J., Loehr, T. M., and Ortiz de Montellano, P. R. (1996) Biochemistry 35, 12788-12795.
23. Dawson, J. (1988) Science 240, 433-439.
24. Rietjens, I. M. C. M., Osman, A. M., Veeger, C., Zakharieva, O., Antony, J., Grodzicki, M., and Trautvvein, A. X. (1996) J. Biol. Inorg. Chem. 1, 372-376.
25. Finzel, B. C., Poulos, T. L., and Kraut, J. (1984) J. Biol. Chem. 259, 13027-13036.
26. Poulos, T. L., Finzel, B. C., Gunsalus, I. C., Wagner, G. C., and Kraut, J. (1985) J. Biol. Chem. 260, 16122-16130.
27. Yeung, B. K., Wang, X., Sigman, J. A., Petillo, P. A., and Lu, Y. (1997) Chem. Biol. 4, 215-221.
28. Huff, A. M., Chang, C. K., Cooper, D. K., Smith, K. M., and Dawson, J. H. (1993) Inorg. Chem. 32, 1460-1466.
29. Andersson, L. A. (1982) Tlie Active Site Environments of Heme Mono-oxygenases: Spectroscopic Investigations of Cytochrome P450 and Secondary Amine Mono-oxygenase, Ph.D. Thesis, University of South Carolina, Columbia, SC.
30. Dawson, J. H., Andersson, L. A., and Sono, M. (1982) J. Biol. Chem. 257, 3606-3617.
31. Dawson, J. H., Andersson, L. A., and Sono, M. (1992) New J. Chem. 16, 577-582.
32. Vickery, L., Salmon, A., and Sauer, K. (1975) Biochim. Biophys. Acta 386, 87-89.
33. Lipscomb, J. D. (1980) Biochemistry 19, 3590-3599.
34. Hollenberg, P. F., Hager, L. P., Blumberg, W. E., and Peisach, J. (1980) J. Biol. Chem. 255, 4801-4807.
35. Yonetani, T., and Anni, H. (1987) J. Biol. Chem. 262, 9547-9554.
36. Sono, M., Dawson, J. H., Hall, K., and Hager, L. P. (1986) Biochemistry 25, 347-356.
37. Erman, J. E. (1974) Biochemistry 13, 39-44.
38. Sono, M., Hager, L. P., and Dawson, J. H. (1991) Biochim. Biophys. Acta 1078, 351-359.
39. Collman, J. P., Sorrell, T. N., and Hoffman, B. M. (1975) J. Am. Chem. Soc. 97, 913-914.
40. Koch, S., Tang, S. C., Holm, R. H., Frankel, R. B., and Ibers, J. A. (1975) J. Am. Chem. Soc. 97, 916-918.
41. Koch, S., Tang, S. C., Holm, R. H., and Frankel, R. B. (1975) J. Am. Chem. Soc. 97, 914-916.
42. Poulos, T. L. (1996) J. Biol. Inorg. Chem. 1, 356-359.
43. Goodin, D. B. (1996) J. Biol. Inorg. Chem. 1, 360-363.
44. Sundaramoorthy, M., Temer, J., and Poulos, T. L. (1995) Structure 3, 1367-1377.
45. Ueno, T., Kousumi, Y., Yoshizawa-Kumagaye, K., Nakajima, K., Ueyama, N., Okamura, T.-a., and Nakamura, A. (1998) J. Am. Chem. Soc. 120, 12264-12273.
46. Cupp-Vickery, J. R., and Poulos, T. L. (1995) Nat. Struct. Biol. 2, 144-153.
47. Hasemann, C. A., Ravichandran, K. G., Peterson, J. A., and Deisenhofer, J. (1994) J. Mol. Biol. 236, 1169-1185.
48. Ravichandran, K. G., Boddupalli, S. S., Hasemann, C. A., Peterson, J. A., and Deisenhofer, J. (1993) Science 261, 731-736.
49. Goodin, D. B., and McRee, D. E. (1993) Biochemistry 32, 3313-3324.
50. Tang, S. C., Koch, S., Papaefthymiou, G. C., Foner, S., Frankel, R. B., Ibers, J. A., and Holm, R. H. (1976) J. Am. Chem. Soc. 98, 2414-2434.
51. Dawson, J. H., and Sono, M. (1987) Chem. Rev. 87, 1255-1276.
52. Tsai, R., Yu, C. A., Gunsalus, I. C., Peisach, J., Blumberg, W., Orme-Johnson, W. H., and Beinert, H. (1970) Proc. Natl. Acad. Sei. U.S.A. 66, 1157-1163.
53. Ozols, J., and Strittmatter, P. (1964) J. Biol. Chem. 239, 1018-1023.
54. Lloyd, E., Hildebrand, D. P., Tu, K. M., and Mauk, A. G. (1995) J. Am. Chem. Soc. 117, 6434-6438.
55. McKnight, J., Cheesman, M. R., Thomson, A. J., Miles, J. S., and Munro, A. W. (1993) Eur. J. Biochem. 213, 683-687.
56. Reynolds, M. F., Shelver, D., Kerby, R. L., Parks, R. B., Roberts, G. P., and Burstyn, J. N. (1998) J. Am. Chem. Soc. 120, 9080-9081.
57. Chevion, M., Peisach, J., and Blumberg, W. E. (1977) J. Biol. Chem. 252, 3637-3645.
58. Martinis, S. A., Sotiriou, C., and Chang, C. K. (1989) Biochemistry 28, 879-884.
59. Blumberg, W. E., Peisach, J., Wittenberg, B. A., and Wittenberg, J. B. (1968) J. Biol. Chem. 243, 1854-1862.
60. Chang, C. K., and Dolphin, D. (1975) J. Am. Chem. Soc 20, 5948-5950.
61. Yu, C.-A., and Gunsalus, I. C. (1974) J. Biol. Chem. 249, 94-101.
62. Hollenberg, P. F., and Hager, L. P. (1973) J. Biol. Chem. 248, 2630-2633.
63. Griffin, B. W., Peterson, J. A., and Estabrook, R. W. (1979) in The Porphyrins (Dolphin, D., Ed.) Vol. 7, pp 333-375, Academic Press, New York.
64. Shiro, Y., Fujii, M., Isogai, Y., Adachi, S.-i., lizuka, T., Obayashi, E., Makino, R., Nakahara, K., and Shoun, H. (1995) Biochemistry 34, 9052-9058.