The reduction potential of cytochrome b5 is modulated by its exposed heme edge

Biochemistry

Volumn 37, Issue 6, 1998, Pages 1485-1494

  Rivera, Mario ^a   Seetharaman, Rajalakshmi ^a   Girdhar, Deepak ^a   Wirtz, Marc ^a   Zhang, Xuejun ^b   Wang, Xioqiang ^b   White, Steven ^a  

^a OKLAHOMA STATE UNIVERSITY   (United States)

^b OKLAHOMA MEDICAL RESEARCH FOUNDATION   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B5;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; MITOCHONDRIAL MEMBRANE; MOLECULAR DYNAMICS; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; RAT;

AMINO ACID SUBSTITUTION; ANIMALS; CRYSTALLOGRAPHY, X-RAY; CYTOCHROMES B5; ELECTRIC CONDUCTIVITY; ELECTRODES; HEME; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; POTENTIOMETRY; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; WATER;

EID: 0032502023     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972390g     Document Type: Article

References (49)

1. Eddowes, M. J., and Hill, H. A. O. (1977) J. Chem. Soc., Chem. Commun., 771-772.
2. Armstrong, F. A., Hill, H. A. O., and Walton, N. J. (1988) Acc. Chem. Res. 21, 407.
3. Taniguchi, I., Toyosawa, K., Yamaguchi, H., and Yasukouchi, K. (1982) J. Chem. Soc., Chem. Commun., 1032.
4. Taniguchi, I., Toyosawa, K., Yamaguchi, H., and Yasukouchi, K. (1982) J. Electroanal. Chem. 140, 187.
5. Armstrong, F. A. (1990) Struct. Bonding (Berlin) 72, 137-221.
6. Bond, A. M. (1994) Inorg. Chim. Acta 226, 293-340.
7. Hawkridge, F. M., and Taniguchi, I. (1995) Comments Inorg. Chem. 17, 163-187.
8. Hill, H. A. O., Page, D. J., Walton, N. J., and Whitford, D. (1985) J. Electroanal. Chem. 187, 315-324.
9. Bond, A. M., Hill, H. A. O., Page, D. J., Psalti, I. S. M., and Walton, N. J. (1990) Eur. J. Biochem. 191, 737-742.
10. Bagby, S., Barker, P. D., Di Gleria, K., Hill, H. A. O., and Lowe V. J. (1988) Biochem. Soc. Trans., 958-959.
11. Armstrong, F. A., Hill, H. A., and Oliver, B. N. J. (1984) J. Chem. Soc., Chem. Commun., 976-977.
12. Armstrong, F. A., Hill, H. A. O., Oliver, B. N., and Walton, N. J. (1984) J. Am. Chem. Soc. 106, 921-923.
13. Armstrong, F. A., Hill, H. A. O., Oliver, B. N., and Whitford, D. (1985) J. Am. Chem. Soc. 107, 1473-1476.
14. Rivera, M., Wells, M. A., and Walker, F. A. (1994) Biochemistry 33, 2161-2170.
15. Glenn, J. D., and Bowden, E. F. (1996) Chem. Lett., 399-400.
16. Armstrong, F. A., Cox, P. A., Hill, H. A. O., Lowe, V. J., and Oliver, B. N. (1987) J. Electroanal. Chem. 217, 331-366.
17. Rivera, M., Barillas-Mury, C., Christensen, K. A., Little, J. W., Wells, M. A., and Walker, F. A. (1992) Biochemistry 31, 12233-12240.
18. Bodman, S. B., Schuler, M. A., Jollie, D. R., and Sugar, S. G (1986). Proc. Natl. Acad. Sci. U.S.A. 83, 9443-9447.
19. Tominaga, M., Yanagimoto, J., Nassar, A. E. F., Rusling, J. F., and Nakashima, N. (1996) Chem. Lett., 523-524.
20. Walker, F. A., Emrick, D., Rivera, J. E., Hanquet, B. J., and Buttlaire, D. H. (1988) J. Am. Chem. Soc. 110, 6234-6240.
21. Kurumaya, K., Okazaki, T., Seido, N., Akasaka, Y., Kawajiri, Y., and Kajiwara, M. (1988) J. Labelled Compd. Radiopharm. 27, 217-235.
22. Bunce, R. A., Shilling, C. L., III, and Rivera, M. (1997) J. Labelled Compd. Radiopharm. 34, 669-675.
23. Rivera, M., and Walker, F. A. (1995) Anal. Biochem. 230, 295-302.
24. Rodríguez-Marañón, M. J., Qiu, F., Stark, R. E., White, S. P., Zhang, X., Foundling, S. I., Rodríguez. V., Schilling, C. L., III, Bunce, R. A., and Rivera, M. (1996) Biochemistry 35, 16378-16390.
25. Teale, F. W. J. (1959) Biochim. Biophys. Acta 35, 543.
26. Reid, L. S., Mauk, M. R., and Mauk, A. G. (1984) J. Am. Chem. Soc. 106, 2182-2185.
27. Durley, R. C. E., and Mathews, F. S. (1996) Acta Crystallogr. D52, 65-72.
28. Guillemette, J. G., Barker, P. D., Eltis, L. D., Lo, T. P., Smith, M., Brayer, G. D., and Mauk, A. G. (1994) Biochimie 76, 592-604.
29. Mauk, A. G., Mauk, M. R., Moore, G. R., and Northrup, S. H. (1995) J. Bioenerg. Biomembr. 27, 311-330.
30. Rodgers, K. K., Pochapsky, T. C., and Sugar, S. G. (1988) Science 240, 1657-1659.
31. Lee, K. B., Jun, E., La Mar, G. N., Rezzano, I. N., Pandey, R. K., Smith, K. M., Walker, F. A., and Buttlaire, D. H. (1991) J. Am. Chem. Soc. 113, 3576-3583.
32. Rodgers, K. K., and Sligar, S. G. (1991) J. Am. Chem. Soc. 113, 9419-9421.
33. Rodgers, K. K., and Sligar, S. G. (1991) J. Mol. Biol. 221, 1453-1460.
34. McLean, M. A., and Sligar, S. G. (1995) Biochem. Biophys. Res. Commun. 215, 316-320.
35. Zhang, X., and Mathews, B. W. (1994) Acta Crystallogr. D50, 675-686.
36. Tronrud, D. E., Ten Eyck, L. F., and Mathews, B. W. (1987) Acta Crystallogr. A43, 489-503.
37. Brunger, A. T. (1992) in X-PLOR version 3.1: A system for X-ray Crystallography and NMR, Yale University Press, New Haven, CT.
38. Brunger, A. T. (1992) Nature 335, 472-474.
39. Laskowski, R. A., McArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
40. Kassner, R. J. (1972) Proc. Natl. Acad. Sci. U.S.A. 69, 2263-2267.
41. Kassner, R. J. (1973) J. Am. Chem. Soc. 95, 2674-2677.
42. Churg, A. K., and Warshel, A. (1986) Biochemistry 25, 1675-1681.
43. Mueller, E. J., Loida, P. J., and Sligar, S. G. (1995) in Cytochrome P450, Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P. R., Ed.) 2nd ed., pp 83-124, Plenum Press, New York.
44. Cullison, J. K., Hawkridge, F. M., Nakashima, N., and Yoshikawa, S. (1994) Langmuir 10, 877-882.
45. Nassar, A. E. F., Narikiyo, Y., Sagara, T., Nakashima, N., and Rusling, J. (1995) J. Chem. Soc., Faraday Trans. 91, 1775-1782.
46. Nassar, A. E. F., Willis, W. S., and Rusling, J. F. (1995) Anal. Chem. 67, 2386-2392.
47. Bianco, P., and Haladjian, J. (1997) Electrochim. Acta 42, 587-594.
48. Zhang, Z., Nassar, A. E. F., Lu, Z., Schenkman, J. B., and Rusling, J. F. (1997) J. Chem. Soc., Faraday Trans. 93, 1769-1774.
49. Kazlauskaite, J., Westlake, A. C. G., Wong, L. L., and Hill, H. A. O. (1996) J. Chem. Soc., Chem. Commun., 2189-2190.