Kinetics of Reduction by Free Flavin Semiquinones of the Components of the Cytochrome c-Cytochrome c Peroxidase Complex and Intracomplex Electron Transfer

Biochemistry

Volumn 26, Issue 10, 1987, Pages 2836-2848

  Poulos, Thomas L ^a   Tollin, Gordon ^a   Hazzard, James T ^a  

^a UNIVERSITY OF ARIZONA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; CYTOCHROME C PEROXIDASE; DRUG DERIVATIVE; FLAVIN SEMIQUINONE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; PEROXIDASE;

ANIMAL; ARTICLE; ELECTRON TRANSPORT; ENZYMOLOGY; HORSE; KINETICS; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; TUNA;

ANIMAL; CYTOCHROME C; CYTOCHROME-C PEROXIDASE; ELECTRON TRANSPORT; FLAVIN MONONUCLEOTIDE; FLAVIN-ADENINE DINUCLEOTIDE; HORSES; KINETICS; OXIDATION-REDUCTION; PEROXIDASES; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SUPPORT, U.S. GOV'T, P.H.S.; TUNA;

EID: 0023659397     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00384a027     Document Type: Article

References (67)

1. Ahmad, I., Cusanovich, M. A., & Tollin, G. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 6724–6728.
2. Ahmad, I., Cusanovich, M. A., & Tollin, G. (1982) Biochemistry 21, 3122–3128.
3. Bechtold, R., & Bosshard, H. R. (1985) J. Biol. Chem. 260, 5191–5200.
4. Bhattacharyya, A., Tollin, G., McIntire, W., & Singer, T. P. (1985) Biochem. J. 228, 337–345.
5. Bhattacharyya, A., Meyer, T. E., & Tollin, G. (1986) Biochemistry 25, 4655–4561.
6. Bickar, D., Turrens, J. F., & Lehninger, A. L. (1985) Fed. Proc., Fed. Am. Soc. Exp. Biol. 44, 678.
7. Bisson, R., & Capaldi, R. A. (1981) J. Biol. Chem. 256, 4362–4367.
8. Blankenhorn, G. (1976) Eur. J. Biochem. 67, 67–80.
9. Cheung, E., Taylor, K., Kornblatt, J. A., English, A. M., McLendon, G., & Miller, J. R. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 1330–1333.
10. Conroy, C. W., Tyma, P., Daum, P. H., & Erman, J. E. (1978) Biochim. Biophys. Acta 537, 62–69.
11. Crutchley, R. J., Ellis, W. R., Jr., & Gray, H. B. (1985) J. Am. Chem. Soc. 107, 5002–5004.
12. Cusanovich, M. A., & Tollin, G. (1980) Biochemistry 19, 3343–3347.
13. Cusanovich, M. A., Meyer, T. E., & Tollin, G. (1985) Biochemistry 24, 1281–1287.
14. Dickerson, J. L., Kornuc, J. J., & Rees, D. C. (1985) J. Biol. Chem. 260, 5175–5178.
15. Draper, R. D., & Ingraham, L. L. (1968a) Arch. Biochem. Biophys. 139, 265–268.
16. Draper, R. D., & Ingraham, L. L. (1968b) Arch. Biochem. Biophys. 125, 802–808.
17. Goodin, D. B., Mauk, A. G., & Smith, M. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 1295–1299.
18. Hazzard, J. T., Cusanovich, M. A., Getzoff, E. D., Tainer, J., & Tollin, G. (1986) Biochemistry 25, 3318–3328.
19. Henderson, R. W., & Rawlinson, W. A. (1961) in Haematin Enzymes (Falk, J. E., Remberg, R., & Morton, R. K., Eds.) pp 370–381, Pergamon, New York.
20. Higuchi, Y., Bando, S., Kusunoki, M., Matsuura, Y., Yasuoka, N., Kakudo, M., Yamanaka, T., Yagi, T., & Inokuchi, H. (1981) J. Biochem. (Tokyo) 89, 1659–1662.
21. Ho, P. S., Hoffman, B. M., Kang, C. H., & Margoliash, E. (1983) J. Biol. Chem. 258, 4356–4363.
22. Ho, P. S., Sutoris, C., Liang, N., Margoliash, E., & Hoffman, B. M. (1985) J. Am. Chem. Soc. 107, 1070–1071.
23. Hoffman, B. M., Roberts, J. E., Brown, T. G., Kang, C. H., & Margoliash, E. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 6132–6136.
24. Hoffman, B. M., Roberts, J. E., Kang, D. H., & Margoliash, E. (1981) J. Biol. Chem. 256, 6556–6564.
25. Hori, T., & Kamen, M. D. (1961) Biochim. Biophys. Acta 48, 266–286.
26. Hori, H., & Yonetani, T. (1985) J. Biol. Chem. 260, 349–355.
27. Hoth, L. R., & Erman, J. E. (1984) Biochim. Biophys. Acta 788, 151–153.
28. Jones, A. (1978) J. Appl. Crystallogr. 11, 268–272.
29. Kang, C. H., Ferguson-Miller, S., & Margoliash, E. (1977) J. Biol. Chem. 252, 919–926.
30. Kang, C. H., Brautigan, D. L., Osherhoff, N., & Margoliash, E. (1978) J. Biol. Chem. 253, 6502–6510.
31. Kang, D. S., & Erman, J. E. (1982) J. Biol. Chem. 257, 12775–12779.
32. Matthew, J. B., & Richards, F. M. (1982) Biochemistry 21, 4989–4999.
33. Matthew, J. B., Hanania, G. H. I., & Gurd, F. R. N. (1979) Biochemistry 18, 1919–1928.
34. Matthew, J. B., Weber, P. C., Salemme, F. R., & Richards, F. M. (1983) Nature (London) 301, 169–171.
35. McLendon, G., Guarr, T., McGuire, M., Simolo, K., Strauch, S., & Taylor, K. (1985) Coord. Chem. Rev. 64, 113–124.
36. Meyer, T. E., & Kamen, M. (1982) Adv. Protein Chem. 35, 105–212.
37. Meyer, T. E., Przysiecki, C. T., Watkins, J. A., Bhattacharyya, A., Simondsen, R. P., Cusanovich, M. A., & Tollin, G. (1983) Proc. Natl. Acad. Sci. U.S.A. 80, 6740–6744.
38. Meyer, T. E., Watkins, J. A., Przysiecki, C. T., Tollin, G., & Cusanovich, M. A. (1984) Biochemistry 23, 4761–4767.
39. Mochan, E., & Nicholls, P. (1972) Biochim. Biophys. Acta 267, 309–319.
40. Moench, S. J. (1984) Ph.D. Dissertation, Colorado State University.
41. Myers, D., & Palmer, G. (1985) J. Biol. Chem. 260, 3887–3890.
42. Nelson, C. E., Sitzman, E. V., Kang, C. H., & Margoliash, E. (1977) Anal. Biochem. 83, 622–631.
43. Nicholls, P., & Mochan, E. (1971) Biochem. J. 121, 66–67.
44. Peisach, J., Blumberg, W. E., Wittenberg, B. A., & Wittenberg, J. B. (1968) J. Biol. Chem. 243, 1871–1880.
45. Peterson-Kennedy, S. E., McGourty, J. L., Ho, P. S., Sutoris, C. J., Liang, N., Zemel, H., Blough, N. V., Margoliash, E., & Hoffman, B. M. (1985) Coord. Chem. Rev. 64, 125–133.
46. Pettigrew, G. W., & Seilman, S. (1982) Biochem. J. 201, 9–18.
47. Postgate, J. R. (1956) J. Gen. Microbiol. 14, 545–572.
48. Poulos, T. L., & Kraut, J. (1980) J. Biol. Chem. 255, 10322–10330.
49. Poulos, T. L., & Mauk, A. G. (1983) J. Biol. Chem. 258, 7369–7373.
50. Poulos, T. L., & Finzel, B. C. (1984) Pept. Protein Rev. 4, 115–171.
51. Przysiecki, C. T., Bhattacharyya, A., Tollin, G., & Cusanovich, M. A. (1985) J. Biol. Chem. 260, 1452–1458.
52. Purcell, W. L., & Erman, J. E. (1976) J. Am. Chem. Soc. 98, 7033–7037.
53. Salemme, F. R. (1976) J. Mol. Biol. 102, 563–568.
54. Salemme, F. R. (1978) Annu. Rev. Biochem. 46, 299–329.
55. Scholes, C. P., & Malmstrom, B. G. (1986) FEBS Lett. 198, 125–129.
56. Shire, S. J., Hanania, G. I. H., & Gurd, F. R. N. (1974) Biochemistry 13, 2967–2974.
57. Simondsen, R. P., & Tollin, G. (1983) Biochemistry 22, 3008–3016.
58. Simondsen, R. P., Weber, P. C., Salemme, F. R., & Tollin, G. (1982) Biochemistry 21, 6366–6375.
59. Smith, W. W., Burnett, R. M., Darling, G. D., & Ludwig, M. L. (1977) J. Mol. Biol. 117, 195–225.
60. Tanford, C., & Roxby, R. (1972) Biochemistry 11, 2192–2195.
61. Tollin, G., Cheddar, G., Watkins, J. A., Meyer, T. E., & Cusanovich, M. A. (1984) Biochemistry 23, 6345–6349.
62. Tollin, G., Hanson, L. K., Caffrey, M., Meyer, T. E., & Cusanovich, M. A. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 3693–3697.
63. Waldmeyer, B., & Bosshard, H. R. (1985) J. Biol. Chem. 260, 5184–5190.
64. Waldmeyer, B., Bechtold, R., Bosshard, H. R., & Poulos, T. L. (1982) J. Biol. Chem. 257, 6073–6076.
65. Wittenberg, B., Kampa, L., Wittenberg, J. B., Blumberg, W. E., & Peisach, J. (1968) J. Biol. Chem. 243, 1863–1870.
66. Yonetani, T. (1967) Methods Enzymol. 1, 336–339.
67. Yonetani, T. (1976) Enzymes (3rd Ed.) 18C, 345–361.