Expression and characterization of recombinant human cytochrome c in E. coli

Journal of Bioenergetics and Biomembranes

Volumn 34, Issue 6, 2002, Pages 423-431

  Jeng, Wen Yih ^a   Chen, Chiu Yueh ^a   Chang, Hsien Chang ^a   Chuang, Woei Jer ^a  

^a NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

Author keywords

Assignment; Folding; Heme proteins; Heteronuclear; NMR; Protein expression

Indexed keywords

CYTOCHROME C; RECOMBINANT PROTEIN;

ARTICLE; CYCLIC POTENTIOMETRY; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION POTENTIAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BASE SEQUENCE; CYTOCHROME C GROUP; DNA, RECOMBINANT; ELECTROCHEMISTRY; ESCHERICHIA COLI; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY;

BACTERIA (MICROORGANISMS); EQUUS CABALLUS; ESCHERICHIA COLI;

EID: 0036963585     PISSN: 0145479X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022561924392     Document Type: Article

References (40)

1. Adrain, C., and Martin, S. J. (2001). Trends Biochem. Sci. 26. 390-397.
2. Banci, L., Bertini, I., Rosato, A., and Varani, G. (1999). J. Biol. Inorg. Chem. 4, 824-837.
3. Baxter, S. M., and Fetrow, J. S. (1999). Biochemistry 38, 4493-4503.
4. Benavides-Garcia, M. G., Rivera, E. V., Ramos, W., Hinck, A. P., and Nall, B. T. (2002). J. Biomol. NMR 22, 93-94.
5. Cavanagh, J., Fairbrother, W. J., Palmer, A. G., and Skelton, N. J. (1996). Protein NMR Spectroscopy, Academic Press, San Diego, CA.
6. Clore, G. M., and Gronenbom, A. M. (1998). Trends Biotechnol. 16, 22-34.
7. Fesik, S. W., and Zuiderweg, E. R. P. (1988). J Magn. Reson. 78, 588-593.
8. Grzesiek. S., Anglister, J., and Bax, A. (1993). J. Magn. Reson. B 101, 114-119.
9. Grzesiek, S., and Bax, A. (1992a). J. Magn. Reson. 96, 432-440.
10. Grzesiek, S., and Bax, A. (1992b). J. Am. Chem. Soc. 114, 6291-6293.
11. Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T., and Masliah, E. (1999). J. Biol. Chem. 274. 28849-28852.
12. Ikura, I., Kay, L. E., and Bax, A. (1991). J. Biomol. NMR 1, 299-304.
13. Kane, J. F. (1995). Curr. Opin. Biotechnol. 6, 494-500.
14. Khan, S. M., Cassarino, D. S., Abramova, N. N., Keeney, P. M., Borland, M. K., Trimmer, R A., Krebs, C. T., Bennett, J. C., Parks, J. K., Swerdlow, R. H., Parker, W. D., Jr., and Bennett, J. P., Jr. (2000). Ann. Neurol. 48, 148-155.
15. Kluck, R. M., Bossy-Wetzel, E., Green, D. R., and Newmeyer, D. D. (1997). Science 275, 1132-1136.
16. Korszun, Z. R., Moffat, K., Frank, K., and Cusanovich, M. A. (1982). Biochemistry 21, 2253-2258.
17. Kurland, C., and Gallant, J. (1996). Curr. Opin. Biotechnol. 7, 489-493.
18. Marion, D., Driscoll, P. C., Kay, L. E., Wingfield, P. T., Bax, A. Gronenborn, A. M., and Clore, G. M. (1989). Biochemistry 28, 6150-6156.
19. Moore, G. R., and Pettigrew, G. W. (1990). Cytochromes c. Evolutionary, Structural, and Physicochemical Aspects, Springer-Verlag, New York.
20. Morar, A. S., Kakouras, D., Young, G. B., Boyd, J., and Pielak, G. J. (1999). J. Biol. Inorg. Chem. 4, 220-222.
21. Muhandiram, D. R., and Kay, L. E. (1994). J. Magn. Reson. B 103, 203-216.
22. Olson, M., and Kornbluth, S. (2001). Curr. Mol. Med. 1, 91-122.
23. Patel, C. N., Lind, M. C., and Pielak, G. J. (2001). Protein Expr. Purif. 22, 220-224.
24. Pettigrew, G. W., and Moore, G. R. (1987). Cytochromes c. Biological Aspects, Springer-Verlag, New York.
25. Pollock, W. B., Rosell, F. I., Twitchett, M. B., Dumont, M. E., and Mauk, A. G. (1998). Biochemistry 37, 6124-6131.
26. Price, N. J., Brennan, L., Faria, T. Q., Vijgenboom, E, Canters, G. W., Turner, D. L., and Santos, H. (2000). Protein Expr. Purif, 20, 444-450.
27. Qi, R. X., Beckman, R. A., and Wand, A. J. (1996). Biochemistry 35, 12275-12286.
28. Qi, P. X., Di Stefano, D. L., and Wand, A. J. (1994). Biochemistry 33, 6408-6417.
29. Scott, R. A., and Mauk, A. G. (1996). Cytochrome c. A Multidisciplinary Approach, University Science Books, Sausalito, CA.
30. Shi, Y. (2001). Nat. Struct. Biol. 8, 394-401.
31. Szabo, C. M., Sanders, L. K., Le, H. C., Chien, E. Y., and Oldfield, E. (2000). FEBS Lett. 482, 25-30.
32. Tanaka, Y., Ashikari, T., Shibano, Y., Amachi, T., Yoshizumi, H., and Matsubara. H. (1988). J. Biochem. 103, 954-961.
33. Thomas, P. E., Ryan, D., and Levin, W. (1976). Anal. Biochem. 75, 168-176.
34. Tomlinson, E. J., and Ferguson, S. J. (2000). J. Biol. Chem., 275, 32530-32534.
35. Wand, A. J., and Englander, S. W. (1996). Curr Opin. Biotechnol. 7, 403-408.
36. Wang, A. C., Lodi, P. J., Qin, J., Vuister, G. W., Gronenborn, A. M., and Clore, G. M. (1994). J. Magn. Reson. B 105, 196-198.
37. Wittekind. M., and Mueller. L. (1993). J. Magn. Reson. 101, 201-205.
38. Worrall, J. A., Kolczak, U., Canters, G. W., and Ubbink, M. (2001). Biochemistry 40, 7069-7076.
39. Wuthrich, K. (1986). NMR of Proteins and Nucleic Acid, Wiley, New York.
40. Zalewski, A., Goldberg, S., Krol, R., and Maroko, P. R. (1987). Am. Heart J. 113, 124-129.