Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase

Journal of the American Chemical Society

Volumn 125, Issue 39, 2003, Pages 11788-11789

  Chen, Dawei ^a   Walsby, Charles ^b   Hoffman, Brian M ^b   Frey, Perry A ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE 2,3 AMINOMUTASE; MUTASE; S ADENOSYLMETHIONINE; SELENOMETHIONINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CLUSTER ANALYSIS; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; SPECTROSCOPY; X RAY SPECTROMETRY;

ELECTRON SPIN RESONANCE SPECTROSCOPY; INTRAMOLECULAR TRANSFERASES; IRON-SULFUR PROTEINS; S-ADENOSYLMETHIONINE;

EID: 0141620318     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja036120z     Document Type: Article

References (31)

1. Frey, P. A.; Magnusson, O. Th. Chem. Rev. 2003, 103, in press.
2. Moss, M. L.; Frey, P. A. J. Biol. Chem. 1987, 262, 14859.
3. Baraniak, J.; Moss, M. L.; Frey, P. A. J. Biol. Chem. 1989, 264, 1357.
4. Ballinger, M. D.; Frey, P. A.; Reed, G. H. Biochemistry 1992, 31, 10782.
5. Ballinger, M. D.; Frey, P. A.; Reed, G. H.; LoBrutto, R. Biochemistry 1995, 34, 10086.
6. Chang, C. H.; Ballinger, M. D.; Reed, G. H.; Frey, P. A. Biochemistry 1996, 35, 11081.
7. Wu, W.; Lieder, K. W.; Reed, G. H.; Frey, P. A. Biochemistry 1995, 34, 10532-10537.
8. Wu, W.; Booker, S.; Lieder, K. W.; Bandarian, V.; Reed, G. H.; Frey, P. A. Biochemistry 2000, 39, 9561.
9. Magnusson, O. Th.; Reed, G. H.; Frey, P. A. Biochemistry 2001, 40, 7773.
10. Sofia, H. J.; Chen, G.; Hetzler, B. G.; Reyes-Spindola, J. F.; Miller, N. E. Nucleic Acids Res. 2001, 29, 1097.
11. Petrovich, R. M.; Ruzicka, F. J.; Reed, G. H.; Frey, P. A. J. Biol. Chem. 1991, 266, 7656.
12. Petrovich, R. M.; Ruzicka, F. J.; Reed, G. H.; Frey, P. A. Biochemistry 1992, 31, 10774.
13. Lieder, K. W.; Booker, S.; Ruzicka, F. J.; Beinert, H.; Reed, G. H.; Frey, P. A. Biochemistry 1998, 37, 2578.
14. Ruzicka, F. J.; Lieder, K. W.; Frey, P. A. J. Bacteriol. 2000, 182, 469-476.
15. Cheek, J.; Broderick, J. B. J. Biol. Inorg. Chem. 2001, 6, 209.
16. Broderick, J. B.; Henshaw, T. F.; Cheek, J.; Wojtuszewski, K.; Smith, S. R.; Trojan, M. R.; McGhan, R. M.; Kopf, A.; Kibbey, M.; Broderick, W. E. Biochem. Biophys. Res. Commun. 2000, 269, 451.
17. Rebeil, R.; Nicholson, W. L. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 9038.
18. Tamarit, J.; Mulliez, E.; Meier, C.; Trautwein, A.; Fontecave, M. J. Biol. Chem. 1999, 274, 31291.
19. Sanyal, I.; Cohen, G.; Flint, D. H. Biochemistry 1994, 33, 3625.
20. Méjean, A.; Tse Sum Bui, B.; Florentin, D.; Ploux, O.; Izumi, Y.; Marquet, A. Biochem. Biophys. Res. Commun. 1995, 217, 1231.
21. Ugulava, N. B.; Frederick, K. K.; Jarrett, J. T. Biochemistry 2003, 42, 2708-2719. Cosper, N. J.; Booker, S. J.; Frey, P. A.; Scott, R. A. Biochemistry 2000, 39, 15668.
22. Ugulava, N. B.; Frederick, K. K.; Jarrett, J. T. Biochemistry 2003, 42, 2708-2719. Cosper, N. J.; Booker, S. J.; Frey, P. A.; Scott, R. A. Biochemistry 2000, 39, 15668.
23. Cosper, N. J.; Booker, S. J.; Frey, P. A.; Scott, R. A. Biochemistry 2000, 39, 15668.
24. Walsby, C.; Hong, W.; Broderick, W. E.; Cheek, J.; Ortillo, D.; Broderick, J. B.; Hoffman, B. J. Am. Chem. Soc. 2002. 124, 3143-3151.
25. Walsby, C. J.; Ortillo, D.; Broderick, J. B.; Hoffman, B. J. Am. Chem. Soc. 2002, 124, 11270-11271.
26. 1, 8.6%. The labeled samples of L-methionine were used with ATP and SAM synthetase to produce labeled SAM as previously described, with minor modifications.23,24 35 GHz CW/pulsed EPR and pulsed ENDOR experiments were carried out at 2 K as previously described.
27. Emptage, M. H.; Kent, T. A.; Kennedy, M. C.; Beinert, H.; Münck, E. Proc. Natl. Acad. Sci. U.S.A. 1983, 80, 4674-4678.
28. ENDOR samples were prepared as follows inside an anaerobic chamber. The purified LAM was prepared as described.13,14 Samples (∼90 μM) were reductively incubated with 10 mM dihydrolipoate in the presence of 0.42 mM PLP, 1.0 mM ammonium iron (II) sulfate, and 15% glycerol in 42 mM Epps buffer at pH 8.0 and 37 °C for 4 h. The reductively incubated enzyme was concentrated by ultrafiltration through Microcon 30 (Millipore) to ∼500 μM. The concentrated enzyme was mixed with SAM or labeled SAM in the presence or absence of 6 mM sodium dithionite, transferred to ENDOR sample tubes, and quickly frozen in liquid nitrogen. Iron-sulfur clusters of samples prepared in the absence of dithionite were cryoreduced by γ-irradiation as desribed.23.24 In all samples, the concentrations of the enzyme and SAM were ∼400 μM and 3.7 mM, respectively.
29. 1 = 2.00-2.05.
30. Werst, M. M.; Kennedy, M. C.; Beinert, H.; Hoffman, B. M. Biochemistry 1990, 29, 10526-10532.
31. Kennedy, M. C.; Stout, C. D. Adv. Inorg. Chem. 1992, 38, 323-339.