NMR of Chromatium Vinosum Ferredoxin: Evidence for Structural Inequivalence and Impeded Electron Transfer between the Two [4Fe-4S] Clusters

Biochemistry

Volumn 34, Issue 1, 1995, Pages 194-205

  Huber, J Gaspard ^a   Gaillard, Jacques ^a   Moulis, Jean Marc ^b  

^a Laboratoire des Métalloprotéines ^*  (France)

^b Dept de Biol Molec et Structurale   (France)

Author keywords

[No Author keywords available]

Indexed keywords

FERREDOXIN;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHROMATIUM VINOSUM; ELECTRON TRANSPORT; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; CHROMATIUM; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; FERREDOXINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY;

CHROMATIUM VINOSUM;

EID: 0028936095     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00001a024     Document Type: Article

References (43)

1. Adman, E. T., Sieker, L. C., & Jensen, L. H. (1973) J. Biol. Chem. 248, 3987-3996.
2. Adman, E. T., Sieker, L. C., & Jensen, L. H. (1976) J. Biol. Chem. 251, 3801-3806.
3. Bachofen, R., & Arnon, D. I. (1966) Biochim. Biophys. Acta 120, 259-265.
4. Backes, G., Mino, Y., Loehr, T. M., Meyer, T. E., Cusanovich, M. A., Sweeney, W. V., Adman, E. T., & Sanders-Loehr, J. (1991) J. Am. Chem. Soc. 113, 2055-2064.
5. Bax, A. (1989) Methods Enzymol. 176, pp 151-168.
6. Bax, A., & Davis, D. G. (1985) J. Magn. Reson. 65, 355-360.
7. Bax, A., Freeman, R., & Morris, G. J. (1981) J. Magn. Res. 42, 164-168.
8. Bax, A., Griffey, R. H., & Hawkins, B. L. (1983) J. Am. Chem. Soc. 105, 7188-7190.
9. Bertini, I., Briganti, F., Luchinat, C., Messori, L., Monnanni, R., Scozzafava, A., & Vallini, G. (1992) Eur. J. Biochem. 204, 831-839.
10. Bertini, I., Capozzi, F., Luchinat, C., Piccioli, M., & Vila, A. J. (1994) J. Am. Chem. Soc. 116, 651-660.
11. Blake, P. R., Park, J.-B., Bryant, F. O., Aono, S., Magnuson, J. K., Eccleston, E., Howard, J. B., Summers, M. F., & Adams, M. W. W. (1991) Biochemistry 30, 10885-10895.
12. Busse, S. C., La Mar, G. N., & Howard, J. B. (1991) J. Biol. Chem. 266, 23714-23723.
13. Cammack, R. (1992) Adv. Inorg. Chem. 38, 281-322.
14. Duée, E. D., Fanchon, E., Vicat, J., Sieker, L. C., Meyer, J., & Moulis J.-M. (1994) J. Mol. Biol. 243, 683-695.
15. Eck, R. V., & Dayhoff, M. O. (1966) Science 152, 363-366.
16. Gaillard, J., Moulis, J.-M., & Meyer, J. (1987) Inorg. Chem. 26, 320-324.
17. Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639.
18. Gaillard, J., Moulis, J.-M., Kümmerle, R., & Meyer, J. (1993a) Magn. Res. Chem. 31, S27-S33.
19. Gaillard, J., Quinkal, I., & Moulis, J.-M. (1993b) Biochemistry 32, 9881-9887.
20. Gueron, M., Plateau, P., Kettani, A., & Decorps, M. (1992) J. Magn. Reson. 96, 541-550.
21. Hase, T., Matsubara, H., & Evans, M. C. W. (1977) J. Biochem. (Tokyo) 81, 1745-1749.
22. Henehan, C. J., Pountney, D. L., Zerbe, O., & Vasäk, M. (1993) Protein Sei. 2, 1756-1764.
23. Henikoff, S., & Henikoff, J. G. (1992) Proc. Natl. Acad. Sci. U.S.A. 89, 10915-10919.
24. Macura, S., Hyang, Y., Suter, D., & Emst, R. R. (1981) J. Magn. Reson. 43, 259-281.
25. Matsubara, H., & Saeki, K. (1992) Adv. Inorg. Chem. 38, 223-280.
26. Meyer, J., Moulis, J.-M., Scherrer, N., Gagnon, J., & Ulrich, J. (1993) Biochem. J. 294, 622-623.
27. Mouesca, J.-M., Rius, G., & Lamotte, B. (1993) J. Am. Chem. Soc. 115, 4714-4731.
28. Moulis, J.-M., Auric, P., Gaillard, J., & Meyer, J. (1984) J. Biol. Chem. 259, 11396-11402.
29. Nettesheim, D. G., Harder, S. R., Feinberg, B. A., & Otvos, J. D. (1992) Biochemistry 31, 1234-1244.
30. Otaka, E., & Ooi, T. (1987) J. Mol. Evol. 26, 257-267.
31. Packer, E. L., Sweeney, W. V., Rabinowitz, J. C., Sternlicht, H., & Shaw, E. N. (1977) J. Biol. Chem. 252, 2245-2253.
32. Patt, S. L., & Sykes, B. D. (1972) J. Chem. Phys. 56, 3182-3184.
33. Phillips, W. D., & Poe, M. (1973) in Iron-Sulfur Proteins (Lovenberg, W., Ed.) Vol. II, pp 255-285, Academic Press, New York.
34. Plateau, P., & Guéron, M. (1982) J. Am. Chem. Soc. 104, 7310-7311.
35. Quinkal, I., Davasse, V., Gaillard, J., & Moulis, J.-M. (1994) Protein Eng. 7, 681-687.
36. Saeki, K., Suetsugu, Y., Tokuda, K., Miyatake, Y., Young, D. A., Marrs, B. L., & Matsubara, T. (1991) J. Biol. Chem. 266, 12889-12895.
37. Schmehl, M., Jahn, A., Meyer Zu Vilsendorf, A., Hennecke, S., Masepohl, B., Schuppler, M., Marxer, M., Oelze, J., & Klipp, W. (1993) Mol. Gen. Genet. 241, 602-615.
38. Shaka, A. J., Lee, C. J., & Pines, A. (1988) J. Magn. Reson. 77, 274-293.
39. Smith, E. T., & Feinberg, B. A. (1990) J. Biol. Chem. 265, 5125-5128.
40. States, D. J., Haberkon, R. A., & Ruben, D. J. (1982) J. Magn. Reson. 48, 286-298.
41. Stombaugh, N. A., Sundquist, J. E., Burns, S. H., & Orme-Johnson, W. H. (1976) Biochemistry 15, 2633-2641.
42. Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) J. Mol. Biol. 222, 311-333.
43. Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons, New York, NY.