Iron-sulfur cluster biosynthesis. A comparative kinetic analysis of native and Cys-substituted ISA-mediated [2Fe-2S]2+ cluster transfer to an apoferredoxin target

Biochemistry

Volumn 42, Issue 19, 2003, Pages 5784-5791

  Wu, Shu Pao ^a   Cowan, J A ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CLUSTER TRANSFER REACTIONS;

BINDING ENERGY; PH EFFECTS; PROTEINS; REACTION KINETICS; SUBSTITUTION REACTIONS;

BIOSYNTHESIS;

APOFERREDOXIN; APOPROTEIN; CYSTEINE; IRON SULFUR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; BIOSYNTHESIS; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; HUMAN; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN TARGETING; SCHIZOSACCHAROMYCES POMBE; SPECIES; TEMPERATURE DEPENDENCE;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CATTLE; FERREDOXIN-NADP REDUCTASE; FERREDOXINS; HUMANS; HYDROGEN-ION CONCENTRATION; IRON-SULFUR PROTEINS; KINETICS; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; TEMPERATURE; THERMODYNAMICS; VISCOSITY;

HOMO; HOMO SAPIENS; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE;

EID: 0038629115     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026939+     Document Type: Article

References (25)

1. Rangaraj, P., Shah, V. K., and Ludden, P. W. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 11250-11255.
2. Goodwin, P. J., Agar, J. N., Roll, J. T., Roberts, G. P., Johnson, M. K., and Dean, D. R. (1998) Biochemistry 37, 10420-10428.
3. Aguilar, O. M., Taormino, J., Thony, B., Ramseier, T., Hennecke, H., and Szalay, A. A. (1990) Mol. Gen. Genet. 224, 413-420.
4. Fu, W., Jack, R. F., Morgan, T. V., Dean, D. R., and Johnson, M. K. (1994) Biochemistry 33, 13455-13463.
5. Lill, R., Diekert, K., Kaut, A., Lange, H., Pelzer, W., Prohl, C., and Kispal, G. (1999) Biol. Chem. Hoppe-Seyler 380, 1157-1166.
6. Lill, R., and Kispal, G. (2000) Trends Biochem. Sci. 25, 352- 356.
7. Zheng, L., Cash, V. L., Flint, D. H., and Dean, D. R. (1998) J. Biol. Chem. 273, 13264-13272.
8. Zheng, L., and Dean, D. R. (1994) J. Biol. Chem. 269, 18723- 18726.
9. Takahashi, Y., and Tokumoto, U. (2002) J. Biol. Chem. 277, 28380.
10. Takahashi, Y., and Nakamura, M. (1999) J. Biochem. 126, 917- 926.
11. Hoff, K. G., Silberg, J. J., and Vickery, L. E. (2000) Proc. Natl. Acad. Sci. U.S.A. 97, 7790-7795.
12. Ollagnier-de-Choudens, S., Mattioli, T., Takahashi, Y., and Fontecave, M. (2001) J. Biol. Chem. 276, 22604-22607.
13. Agar, J. N., Krebs, C., Frazzon, J., Huynh, B. H., Dean, D. R., and Johnson, M. K. (2000) Biochemistry 39, 7856-7862.
14. Yuvaniyama, P., Agar, J. N., Cash, V. L., Johnson, M. K., and Dean, D. R. (2000) Proc. Natl. Acad. Sci. U.S.A. 97, 599-604.
15. Muhlenhoff, U., and Lill, R. (2000) Biochim. Biophys. Acta 1459, 370-382.
16. Lange, H., Kaut, A., Kispal, G., and Lill, R. (2000) Proc. Natl. Acad. Sci. U.S.A. 97, 1050-1055.
17. Kispal, G., Csere, P., Prohl, C., and Lill, R. (1999) EMBO J. 18, 3981-3989.
18. Tong, W. H., and Rouault, T. (2000) EMBO J. 19, 5692-5700.
19. Wu, S., Wu, G., Surerus, K. K., and Cowan, J. A. (2002) Biochemistry 41, 8876-8885.
20. Wu, G., Mansy, S. S., Hille, R., Hemann, C. F., Surerus, K. K., and Cowan, J. A. (2002) J. Biol. Inorg. Chem. 7, 526-532.
21. Wu, G., Mansy, S. S., Wu, S.-p., Surerus, K. K., Foster, M. W., and Cowan, J. A. (2002) Biochemistry 41, 5024-5032.
22. Ziegler, G. A., Vonrhein, C., Hanukoglu, I., and Schulz, G. E. (1999) J. Mol. Biol. 289, 981-990.
23. Moulis, J. M., and Meyer, J. M. (1982) Biochemistry 21, 4762.
24. Krebs, C., Agar, J. N., Smith, A. D., Frazzon, J., Dean, D. R., Huynh, B. H., and Johnson, M. K. (2001) Biochemistry 40, 14069-14080.
25. Dyson, H. J., Jeng, M.-F., Tennant, L. L., Slaby, I., Lindell, M., Cui, D.-S., Kuprin, S., and Holmgren, A. (1997) Biochemistry 36, 2622-2636.