The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer

Biochemistry

Volumn 38, Issue 30, 1999, Pages 9735-9745

  Dwyer, Timothy M ^a   Mortl, Simone ^b   Kemter, Kristina ^b   Bacher, Adelbert ^b   Fauq, Abdul ^c   Frerman, Frank E ^a  

^a Children's Hospital Colorado   (United States)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; DEOXYRIBONUCLEOTIDE; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; MEDIUM CHAIN ACYL COENZYME A DEHYDROGENASE; SEMIQUINONE; UBIQUINOL CYTOCHROME C REDUCTASE;

ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; CONTROLLED STUDY; ELECTRON TRANSPORT; HUMAN; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR MODEL; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REACTION ANALYSIS; REACTION TIME; STEADY STATE; STRUCTURE ACTIVITY RELATION; TRANSPORT KINETICS;

ANIMALS; ELECTRON TRANSPORT; ELECTRON-TRANSFERRING FLAVOPROTEINS; FLAVIN-ADENINE DINUCLEOTIDE; FLAVINS; FLAVOPROTEINS; HUMANS; HYDROGEN BONDING; KINETICS; OXIDATION-REDUCTION; PARACOCCUS DENITRIFICANS; SPECTROPHOTOMETRY, ULTRAVIOLET; SWINE;

BACTERIA (MICROORGANISMS); PARACOCCUS DENITRIFICANS; PROKARYOTA;

EID: 0033609440     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9903906     Document Type: Article

References (68)

1. Hauge, J. G. (1956) J. Am. Chem. Soc. 78, 5266-5272.
2. Izai, K., Uchida, Y., Orii, T., Yamamoto, S., and Hashimoto, T. (1992) J. Biol. Chem. 267, 1027-1033.
3. Ikeda, Y., and Tanaka, K. (1983) J. Biol. Chem. 258, 1077-1085.
4. Lenich, A. C., and Goodman, S. I. (1986) J. Biol. Chem. 261, 4090-4096.
5. Frisell, W. R., and McKenzie, C. G. (1964) J. Biol. Chem. 237, 94-98.
6. Gorelick, R. J., Schopfer, L. M., Ballou, D. P., Massey, V., and Thorpe, C. (1985) Biochemistry 24, 6830-6839.
7. Ramsay, R. R., Steenkamp, D. J., and Husain, M. (1987) Biochem. J. 241, 883-892.
8. Tsai, M. H., and Saier, M. H. (1995) Res. Microbiol. 146. 397-404.
9. Roberts, D. L., Salazar, D., Fulmer, J. P., Frerman, F. E., and Kim, J. J. P. (1998) Biochemistry 38, 1977-1989.
10. DuPlessis E. R., Rohlfs, R. J., Hille, R., and Thorpe, C. (1994) Biochem. Mol. Biol. Int. 32, 195-199.
11. Sato, K., Nishina, Y., and Shiga, K. (1996) J. Biochem. (Tokyo) 120, 276-285.
12. Griffin, K. J., Dwyer, T. M., Manning, M. C., Meyer, J. D., Carpenter, J. F., and Frerman, F. E. (1997) Biochemistry 36, 4194-4202.
13. Swenson, R. P., and Chen, D. (1996) in Flavins and Flavoproteins (Stevenson, K. J., Massey, V., and Williams, C. H., Jr., Eds.) pp 516-518, University of Calgary Press, Calgary.
14. Roberts, D. L., Frerman, F. E., and Kim, J. J. P. (1996) Proc. Natl. Acad. Sci. U.S.A. 90, 1670-1676.
15. Griffin, K. J., DeGala, G. D., Eisenreich, W., Muller, F., Bacher, A., and Frerman, F. E. (1998) Eur. J. Biochem. 255, 125-132.
16. Breinlinger, E., Niemz, A., and Rotello, V. M. (1995) J. Am. Chem. Soc. 117, 5379-5380.
17. Niemz, A., Imbriglio, J., and Rotello, V. M. (1997) J. Am. Chem. Soc. 119, 887-892.
18. Salazar, D., Zhang, L., deGala, G. D., and Frerman, F. E. (1997) J. Biol. Chem. 272, 26425-26433.
19. Herrick, K. R., Salazar, D. Goodman, S. I., Finocchiaro, G., Bedzyk, L. A., and Frerman, F. E. (1994) J. Biol. Chem. 269, 32239-32245.
20. Beckmann, J. D., and Frerman, F. E. (1983) J. Biol. Chem. 258, 7563-7569.
21. Watmough, N. J., Loehr, J. P., Drake, S. K., and Frerman, F. E. (1991) Biochemistry 30, 1317-1323.
22. Frerman, F. E. (1987) Biochim. Biophys. Acta 893, 161-169.
23. Barton, D. H. R., and McCombie, S. W. (1975) J. Chem. Soc., Perkin Trans. 1, 1574-1585.
24. Tischler, M., Pfister, K., Babson, R. D., Ladenberg, K., and Flemming, A. J. (1947) J. Am. Chem. Soc. 69, 1487-1492.
25. Beckmann, J., and Frerman, F. E. (1985) Biochemistry 24, 3912-3921.
26. Heyn, M. P., and Weischet, W. O. (1975) Biochemistry 14, 2962-2968.
27. Massey, V. (1991) in Flavins and Flavoproteins 1990 (Curti, B., Ronchi, S., and Zanetti, G., Eds.) pp 59-66, Walter deGruyter and Co., New York.
28. Clark, W. M. (1960) in Oxidation Reduction Potentials of Organic Systems, p 184-203, The Williams and Wilkins Co., Baltimore, MD.
29. Minneart, K. (1965) Biochim. Biophys. Acta 110, 42-56.
30. Husain, M., Stankovich, M. T., and Fox, B. G. (1984) Biochem. J. 219, 1043-1047.
31. McKean, M. C., Beckmann, J. D., and Frerman, F. E. (1983) J. Biol. Chem. 258, 1866-1870.
32. Nishimoto, K., Watanabe, Y., and Yagi, K. (1978) Biochim. Biophys. Acta 526, 34-41.
33. Hsu, M. C., and Woody, R. W. (1971) J. Am. Chem. Soc. 93, 3515-3525.
34. Blauer, G., Sreerama, N., and Woody, R. W. (1993) Biochemistry 32, 6674-6679.
35. Edmondson, D. E., and Tollin, G. (1971) Biochemistry 10, 113-124.
36. Sun, M., Moore, T. A., and Song, P. S. (1972) J. Am. Chem. Soc. 94, 1730-1740.
37. Scola-Nagelschneider, G., and Hemmerich, P. (1972) Z. Naturforsch. Chem. Sci. 27, 1011-1015.
38. Plaut, G. W. E., and Beach, R. L. (1976) in Flavins and Flavoproteins (Singer, T. P., Ed.) pp 737-744, Elsevier Scientific Publishing, Amsterdam.
39. Kim, J. J. P., Wang, M., and Paschke, R. (1993) Proc. Nat. Acad. Sci. U.S.A. 90, 7523-7527.
40. Trievel, R. C., Wang, R., Anderson, V. E., and Thorpe, C. (1995) Biochemistry 34, 8597-8605.
41. Vock, P., Engst, S., Eder, M., and Ghisla, S. (1998) Biochemistry 37, 1848-1860.
42. Engst, S., Vock, P., Wang, M., Kim, J. J. P., and Ghisla, S. (1999) Biochemistry 38, 257-267.
43. Mattevi, A., Schierbeek, A. J., and Hol, W. G. J. (1991) J. Mol. Biol. 220, 975-994.
44. Murthy, Y. V. S. N., and Massey, V. (1995) J. Biol. Chem. 270, 28586-28594.
45. Muller, Y. A., and Schulz, G. E. (1993) Science 259, 965-967.
46. Lu, G., Campbell, W. H., Schneider, G., and Lindqvist, Y. (1994) Structure 2, 809-821.
47. Zhou, Z., and Swenson, R. P. (1995) Biochemistry 34, 3183-3192.
48. Zhou, Z., and Swenson, R. P. (1996) Biochemistry 35, 15980-15988.
49. Swenson, R. P., and Krey, G. D. (1994) Biochemistry 33, 8505-8514.
50. Ludwig, M. L., Pattridge, K. A., Metzger, A. L., and Dixon, M. M., Eren, M., Feng, Y., and Swenson, R. P. (1996) in Flavins and Flavoproteins, 1996 (Stevenson, K. J., Massey, V. and Williams, C. H., Eds) pp 409-418, University of Calgary Press, Calgary.
51. Miller, S. M. (1995) Biochemistry 34, 13066-13073.
52. Massey, V and Hemmerich, P. (1980) Biochem. Soc. Trans. 8, 246-257.
53. Mizzer, J. P., and Thorpe, C. (1981) Biochemistry 20, 4965-4970.
54. Muller, F., Hemmerich, P., Ehrenberg, A., Palmer, G., and Massey, V. (1970) Eur. J. Biochem. 14, 185-196.
55. McKean, M. C., Sealy, R. C., and Frerman, F. E. (1982) in Flavins and Flavoproteins (Massey, V. and Williams, C. H., Eds) pp 614-617, Elsevier, New York.
56. Lowe, H. J., and Clark, W. M. (1956) J. Biol. Chem. 221, 983-992.
57. Byron, C. M., Stankovich, M. T., Husain, M., and Davidson, V. L. (1989) Biochemistry 28, 8582-8587.
58. Pace, C. P., and Stankovich, M. T. (1987) Biochim. Biophys. Acta 911, 267-276.
59. Whitfield, C. D., and Mayhew, S. G. (1974) J. Biol. Chem. 249, 2801-2810.
60. O'Neil, H., Mayhew, S. G., and Butler, G. (1998) J. Biol. Chem. 273, 21015-21024.
61. Gorelick, R. J., and Thorpe, C. (1986) Biochemistry 25, 7092-7098.
62. Roberts, D. L., Frerman, F. E., and Kim, J. J. P. (1996) in Flavins and Flavoproteins, 1996 (Stevenson, K. J., Massey, V. and Williams, C. H., Eds.) pp 523-526, University of Calgary Press, Calgary.
63. Paulsen, K. E., Orville, A. M., Frerman, F. E., Lipscomb, J. D., and Stankovich, M. T. (1992) Biochemistry 31, 11755-11761.
64. Beard, S. E., Goodman, S. I., Bemelen, K., and Frerman, F. E. (1995) Hum. Mol. Gen. 4, 157-161.
65. deRege, P. J., Williams, S. A., and Therien, M. J. (1995) Science 269, 1409-1413.
66. Bertan, D. N., and Onuchic, J. N. (1996) in Protein Electron Transfer (Bendall, D. S., Ed.) Chapter 2, pp 23-42, Bios Scientific Publishers Ltd., Oxford, U.K.
67. Mikkelsen, K. V., Skov, L. K., Nar, H., and Farver, O. (1993)-Proc. Natl. Acad. Sci. U.S.A. 90, 5443-5445.
68. Pai, E., and Schulz, G. E. (1983) J. Biol. Chem. 258, 1752-1757.