Role of methionine 56 in the control of the oxidation-reduction potentials of the Clostridium beijerinckii flavodoxin: Effects of substitutions by aliphatic amino acids and evidence for a role of sulfur- flavin interactions

Biochemistry

Volumn 37, Issue 27, 1998, Pages 9668-9678

  Druhan, Lawrence J ^a   Swenson, Richard P ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALIPHATIC AMINE; AMINO ACID; FLAVODOXIN; FLAVOPROTEIN; METHIONINE; MUTANT PROTEIN; QUERCETIN; SULFUR;

ARTICLE; CLOSTRIDIUM BEIJERINCKII; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; CLOSTRIDIUM; ESCHERICHIA COLI; FLAVIN MONONUCLEOTIDE; FLAVINS; FLAVODOXIN; METHIONINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; RECOMBINANT PROTEINS; SULFUR;

CLOSTRIDIUM BEIJERINCKII;

EID: 0032493389     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980770b     Document Type: Article

References (46)

1. Mayhew, S. G., and Tollin, G. (1992) in Chemistry and Biochemistry of Flavoenzymes III (Müller, F., Ed.) pp 389-426, CRC Press, Boca Raton, FL.
2. Zhou, Z., and Swenson, R. P. (1995) Biochemistry 34, 3183-3192.
3. Zhou, Z., and Swenson, R. P. (1996) Biochemistry 35, 12443-12454.
4. Zhou, Z., and Swenson, R. P. (1996) Biochemistry 35, 15980-15988.
5. Burnett, R. M., Darling, G. D., Kendall, D. S., LeQuesne, M. F., Mayhew, S. G., Smith, W. W., and Ludwig, M. L. (1974) J. Biol. Chem. 249, 4383-4392.
6. Smith, W. W., Burnett, R. M., Darling, G. D., and Ludwig, M. L. (1977) J. Mol. Biol. 117, 195-225.
7. Ludwig, M. L., Pattridge, K. A., Metzger, A. L., Dixon, M. M., Eren, M., Feng, Y., and Swenson, R. P. (1997) Biochemistry 36, 1259-1280.
8. Ludwig, M. L., Dixon, M. M., Pattridge, K. A., and Swenson, R. P. (1994) in Flavins and Flavoproteins 1993 (Yagi, K., Ed.) pp 363-366, Walter de Gruyter and Co., Berlin.
9. Ludwig, M. L., and Luschinsky, C. L. (1992) in Chemistry and Biochemistry of Flavoenzymes III (Müller, F., Ed.) pp 427-466, CRC Press, Boca Raton, FL.
10. Ludwig, M. L., Pattridge, K. A., Eren, M., and Swenson, R. P. (1991) in Flavins and Flavoproteins 1990 (Curti, B., Ronchi, S., and Zanetti, G., Eds.) pp 423-428, Walter de Gruyter and Co., Berlin.
11. Watenpaugh, K. D., Sieker, L. C., and Jensen, L. H. (1976) in Flavins and Flavoproteins 1976 (Singer, T. P., Ed.) pp 405-410, Elsevier Scientific Publishing Co., Amsterdam.
12. Laudenbach, D. E., Straus, N. A., Pattridge, K. A., and Ludwig, M. L. (1988) in Flavins and Flavoproteins 1987 (Edmondson, D. E., and McCormick, D. B., Eds.) pp 249-260, Walter de Gruyter and Co., Berlin.
13. Luschinsky, C. L., Dunham, W. R., Osborne, C., Pattridge, K. A., and Ludwig, M. L. (1991) in Flavins and Flavoproteins 1990 (Curti, B., Ronchi, S., and Zanetti, G., Eds.) pp 409-413, Walter de Gruyter and Co., Berlin.
14. Watt, W., Tulinsky, A., Swenson, R. P., and Watenpaugh, K. D. (1991) J. Mol. Biol. 218, 195-208.
15. Mayhew, S. G., O'Connell, D. P., O'Farrell, P. A., Yalloway, G. N., and Geoghegan, S. M. (1996) Biochem. Soc. Trans. 24, 122-127.
16. Swenson, R. P., and Krey, G. D. (1994) Biochemistry 33, 8505-8514.
17. Eren, M., and Swenson, R. P. (1989) J. Biol. Chem. 264, 14874-14879.
18. Kunkel, A. T., Roberts, J. D., and Zakour, R. A., (1987) Methods Enzymol. 154, 367-382.
19. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
20. Krey, G. D., Vanin, E. F., and Swenson, R. P. (1988) J. Biol. Chem. 244, 15436-15443.
21. Laemmli, U. K. (1970) Nature 227, 680.
22. Mayhew, S. G., and Massey, V. (1969) J. Biol. Chem. 244, 794-802.
23. Whitby, L. G. (1953) Biochem. J. 54, 437-442.
24. Michaelis, L., and Hill, E. S. (1933) J. Gen. Physiol. 16, 859-873.
25. Clark, W. M. (1972) Oxidation Reduction Potentials of Organic Systems, Robert E. Krieger Publishing Co., Huntington, NY.
26. Wassink, J. H., and Mayhew, S. G. (1975) Anal. Biochem. 68, 609-616.
27. Draper, R. D., and Ingraham, L. L. (1968) Arch. Biochem. Biophys. 125, 802-808.
28. Dubourdieu, M., LeGall, J., and Favoudon, V. (1975) Biochim. Biophys. Acta 376, 519-532.
29. Weiner, S. J., Kollman, P. A., Case, D. A., Singh, U. C., Ghio, C., Alagona, G., Profeta, S., Jr., and Weiner, P. (1984) J. Am. Chem. Soc. 106, 765-784.
30. Connolly, M. L. (1983) Science 221, 709-712.
31. Müller, F. (1991) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. I, pp 38-45, CRC Press, Boca Raton, FL.
32. Ghisla, S., Massey, V., Lhoste, J. M., and Mayhew, S. G. (1974) Biochemistry 13, 589-597.
33. Morgan, R. S., Tatsch, C. E., Gushard, R. H., McAdon, J. M., and Warme, P. K. (1978) Int. J. Pept. Protein Res. 11, 209-217.
34. Reid, K. S. C., Lindley, P. F., and Thornton, J. M. (1985) FEBS Lett. 190, 209-213.
35. Barman, B. G., and Tollin, G. (1972) Biochemistry 11, 4746-4754.
36. Dubourdieu, M., MacKnight, M. L., and Tollin, G. (1974) Biochem. Biophys. Res. Commun. 60, 649-655.
37. Leenders, R., van Hoek, A., van Iersel, M., Veeger, C., and Visser, A. J. W. G. (1993) Eur. J. Biochem. 218, 977-984.
38. Genzor, C. B., Perales-Alcon, A., Sancho, J., and Romero, A. (1996) Nat. Struct. Biol. 3, 329-332.
39. Hunter, C. A., and Sanders, J. K. M. (1990) J. Am. Chem. Soc. 112, 5525-5534.
40. Dougherty, D. A. (1996) Science 271, 163-168.
41. Stapley, B. J., Rohl, C. A., and Doig, A. J. (1995) Protein Sci. 4, 2383-2391.
42. Viguera, A. R., and Serrano, L. (1995) Biochemistry 34, 8771-8779.
43. Janin, J., and Chothia, C. (1978) Biochemistry 17, 2943-2948.
44. Carlson, R., and Langerman, N. (1984) Arch. Biochem. Biophys. 229, 440-447.
45. Born, M. (1920) Z. Phys. 1, 45-53.
46. Fox, J. L., Smith, S. S., and Brown, J. R. (1972) Z. Naturforsch. 27B, 1096-1100.