Modulation of the redox potentials of FMN in Desulfovibrio vulgaris flavodoxin: Thermodynamic properties and crystal structures of glycine-61 mutants

Biochemistry

Volumn 37, Issue 23, 1998, Pages 8405-8416

  O'Farrell, Paul A ^a   Walsh, Martin A ^b   McCarthy, Andrew A ^c   Higgins, Timothy M ^c   Voordouw, Gerrit ^c   Mayhew, Stephen G ^a  

^a UNIVERSITY COLLEGE DUBLIN   (Ireland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

FLAVODOXIN;

ARTICLE; CRYSTAL STRUCTURE; DESULFOVIBRIO VULGARIS; ELECTRON TRANSPORT; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS; X RAY ANALYSIS;

AMINO ACID SUBSTITUTION; APOPROTEINS; CRYSTALLOGRAPHY, X-RAY; DESULFOVIBRIO VULGARIS; FLAVIN MONONUCLEOTIDE; FLAVINS; FLAVODOXIN; GLYCINE; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN CONFORMATION; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); DESULFOVIBRIO VULGARIS;

EID: 0032499631     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi973193k     Document Type: Article

References (61)

1. Mayhew, S. G., and Ludwig, M. L. (1975) in The Enzymes (Boyer, P., Ed.) 3rd ed., Vol. 12, pp 57-109, Academic Press, New York.
2. Mayhew, S. G., and Tollin, G. (1992) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) vol. 3, 389-426, CRC Press, Boca Raton, Florida.
3. Ludwig M. L., and Luschinsky, C. L. (1992) in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. 3, 427-466, CRC Press, Boca Raton, Florida.
4. Ludwig, M. L., Schopfer, L. M., Metzger, A. L., Pattridge, K. A., and Massey, V. (1990) Biochemistry 29, 10364-10375.
5. Franken, H.-D., Rüterjans, H., and Müller, F. (1984) Eur. J. Biochem. 138, 481-489.
6. Vervoort, J., Müller, F., Mayhew, S. G., van den Berg, W. A. M., Moonen, C. T. W., and Bacher, A. (1986) Biochemistry 25, 6789-6799.
7. Vervoort, J., Müller, F., LeGall, J., Bacher, A., and Sedlmaier, H. (1985) Eur. J. Biochem. 151, 49-57.
8. Stockman, B. J., Westler, W. M., Mooberry, E. S., and Markley, J. L. (1988) Biochemistry 27, 136-142.
9. Swenson, R. P., and Krey, G. D. (1994) Biochemistry 33, 8505-8514.
10. Zhou, Z., and Swenson, R. P. (1995) Biochemistry 34, 3183-3192.
11. Zhou, Z., and Swenson, R. P. (1996) Biochemistry 35, 12443-12454.
12. Zhou, Z., and Swenson, R. P. (1996) Biochemistry 35, 15980-15988.
13. Moonen, C. T. W., Vervoort, J., and Müller, F. (1984) Biochemistry 23, 4859-4867.
14. Zheng, Y.-J., and Ornstein, R. L. (1996) J. Am. Chem. Soc. 118, 9402-9408.
15. Smith, W. W., Burnett, R. M., Darling, G. D., and Ludwig, M. L. (1977) J. Mol. Biol. 117, 195-225.
16. Watt, W., Tulinsky, A., Swenson, R. P., and Watenpaugh, K. D. (1991) J. Mol. Biol. 218, 195-208.
17. 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.) 409-414, de Gruyter, Berlin.
18. Romero, A., Caldiera, J., LeGall, J., Moura, I., Moura, J. J. G., and Romao, M. J. (1996) Eur. J. Biochem. 239, 190-196.
19. van Mierlo, C. P. M., Lijnzaad, P., Vervoort, J., Müller, F., Berendsen, H. J. C., and de Vlieg J. (1990) Eur. J. Biochem. 194, 185-198.
20. Sharkey, C., Mayhew, S. G., Higgins, T. M., and Walsh, M. A. (1997) in Flavins and Flavoproteins 1996 (Stevenson, K. J., Massey, V., and Williams, C. H., Jr., Eds.) pp 445-448, University of Calgary Press, Calgary.
21. Draper, R. D., and Ingraham, L. Y. (1968) Arch. Biochem. Biophys. 125, 802-808.
22. Laudenbach, D. E., Straus, N. A., Partridge, K. A., and Ludwig, M. L. (1987) Flavins and Flavoproteins 1987 (Edmonson, D. E., and McCormick, D. B., Eds.) pp 249-260, de Gruyter, Berlin.
23. Carr, M. C., Curley, G. P., Mayhew, S. G., and Vordouw, G. (1990) Biochem. Int. 20, 1025-1032.
24. Curley, G. P., Carr, M. C., Mayhew, S. G., and Voordouw, G. (1991) Eur. J. Biochem. 202, 1091-1100.
25. Kunkel, T. A., Roberts, J. D. and Zakour, R. A. (1987) Methods Enzymol. 154, 367-382.
26. Sanger, F., Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5463-5467.
27. Kleiner, D., Wyatt, P., and Merrick, M. J. (1988) J. Gen. Microbiol. 134, 1779-1784.
28. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
29. Pueyo, J. J., Curley, G. P., and Mayhew, S. G. (1996) Biochem. J. 313, 855-861.
30. Wassink, J. M., and Mayhew, S. G. (1975) Anal. Biochem. 68, 609-616.
31. Massey, V., and Hemmerich, P. (1978) Biochemistry 17, 9-16.
32. Stankovich, M. (1980) Anal. Biochem. 109, 295-308.
33. Clark, W. M. (1960) Oxidation Reduction Potentials of Organic Systems, The Williams and Wilkins Co., Baltimore.
34. Michaelis, L. (1932) J. Biol. Chem. 96, 703-715.
35. Walsh, M. A. (1994) Ph.D. Thesis, National University of Ireland.
36. Watenpaugh, K. D., Sieker, L. C., Jensen, L. H., LeGall, J., and Dubourdieu, M. (1972) Proc. Natl. Acad. Sci. U.S.A 69, 3185-3188.
37. Ducruix, A., and Giege, R. (1992) Crystallization of nucleic acids and proteins, IRL Press, Oxford.
38. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326.
39. Fitzgerald, P. M. D. (1988) J. Appl. Crystallogr. 21, 273-278.
40. Collaborative Computational Project, No. 4 (1994) Acta Crystallogr. D50, 760-763.
41. Hendrickson, W. A., and Konnert, J. H. (1980) in Computing in Crystallography (Diamond, R., Ramaseshan, R., and Venkatesan, K., Eds.) Chapter 13, pp 1-23, The Indian Academy of Sciences, Bangalore.
42. Lamzin, V. S., and Wilson, K. S. (1997) Methods Enzymol. 277, 269-305.
43. Brünger, A. T. (1992) Nature 355, 472-475.
44. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. A47, 110-119.
45. Ramachandran, G. N., and Sasisekharan, V. (1968) Adv. Protein Chem. 23, 283-437.
46. Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meuer, E. F. J., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., and Tasumi, M. (1977) J. Mol. Biol. 112, 535-542.
47. Anderson, R. F. (1983) Biochim. Biophys. Acta. 772, 158-162.
48. McDonald, I., and Thornton, J. (1994) J. Mol. Biol. 238, 777-793.
49. Hall, L., Orchard, B., and Tripathy, S. (1987) Int. J. Quantum Chem. 31, 217-242.
50. Müller, F., and Massey, V. (1969) J. Biol. Chem. 244, 4007-4016.
51. Baker, E. N., and Hubbard, R. E. (1984) Prog. Biophys. Mol. Biol. 44, 97-179.
52. Connolly, M. L. (1983) Science 221, 709-712.
53. 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.
54. Knauf, M. A., Löhr, F., Blümel, M., Mayhew, S. G., and Rüterjans, H. (1996) Eur. J. Biochem. 238, 423-434.
55. Hrovat, A., Blümel, M., Löhr, F., Mayhew, S. G., and Rüterjans, H. (1997) J. Biomol. NMR 10, 53-62.
56. McCarthy, A. A. (1997) Ph.D. Thesis, National University of Ireland.
57. Fersht, A. (1985) Enzyme structure and mechanism, p 298, Freeman and Co., New York.
58. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
59. Mayhew, S. G., Foust, G. P., and Massey, V. (1969) J. Biol. Chem. 244, 803-810.
60. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.
61. Wallace, A. C. Laskowski, R. A., and Thornton, J. M. (1995) Protein Eng. 8, 127-134.