A potent, versatile disulfide-reducing agent from aspartic acid

Journal of the American Chemical Society

Volumn 134, Issue 9, 2012, Pages 4057-4059

  Lukesh III, John C ^a   Palte, Michael J ^a   Raines, Ronald T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO GROUP; ASPARTIC ACIDS; BIOLOGICAL MOLECULE; CATION EXCHANGES; DISULFIDE BONDS; DITHIOLS; DITHIOTHREITOL; L-ASPARTIC ACID; NEUTRAL PH; PROTONATED; SMALL MOLECULES; THIOL GROUPS;

AMINO ACIDS;

COVALENT BONDS;

2 AMINO 1,4 DIMERCAPTOBUTANE; ASPARTIC ACID; DISULFIDE; DITHIOBUTYLAMINE; DITHIOL DERIVATIVE; REDUCING AGENT; UNCLASSIFIED DRUG;

ARTICLE; CATION EXCHANGE; CHEMICAL BOND; CONJUGATION; ISOLATION PROCEDURE; PKA;

ASPARTIC ACID; CREATINE KINASE; DISULFIDES; DITHIOTHREITOL; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PAPAIN; STEREOISOMERISM;

EID: 84857874272     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja211931f     Document Type: Article

References (50)

1. Martelli, P. L.; Fariselli, P.; Cadadio, R. Proteomics 2004, 4, 1655-1671.
2. (a) Cleland, W. W. Biochemistry 1964, 3, 480-482.
3. (b) Jocelyn, P. C. Biochemistry of the SH Group: The Occurence, Chemical Properties, Metabolism and Biological Function of Thiols and Disulphides; Academic Press: London, U.K., 1972.
4. (c) Smith, D. J.; Maggio, E. T.; Kenyon, G. L. Biochemistry 1975, 14, 766-771.
5. (d) Ranganathan, S.; Jayaraman, N. Chem. Commun. 1991, 934-936.
6. (e) Burns, J. A.; Butler, J. C.; Moran, J.; Whitesides, G. M. J. Org. Chem. 1991, 56, 2648-2650.
7. (f) Lees, W. J.; Singh, R.; Whitesides, G. M. J. Org. Chem. 1991, 56, 7328-7331.
8. (g) Lamoureux, G. V.; Whitesides, G. M. J. Org. Chem. 1993, 58, 633-641.
9. (h) Singh, R.; Whitesides, G. M. Bioorg. Chem. 1994, 22, 109-115.
10. (i) Gilbert, H. F. Methods Enzymol. 1995, 251, 8-28.
11. (j) Singh, R.; Lamoureux, G. V.; Lees, W. J.; Whitesides, G. M. Methods Enzymol. 1995, 251, 167-173.
12. (k) Getz, E. B.; Xiao, M.; Chakrabarty, T.; Cooke, R.; Selvin, P. R. Anal. Biochem. 1999, 273, 73-80.
13. (l) Cline, D. J.; Redding, S. E.; Brohawn, S. G.; Psathas, J. N.; Schneider, J. P.; Thorpe, C. Biochemistry 2004, 43, 15195-15203.
14. (a) Whitesides, G. M.; Lilburn, J. E.; Szajewski, R. P. J. Org. Chem. 1977, 42, 332-338.
15. (b) Snyder, J. P.; Carlsen, L. J. Am. Chem. Soc. 1977, 99, 2931-2942.
16. (c) Rosenfield, R. E.; Parthasarathy, R.; Dunitz, J. D. J. Am. Chem. Soc. 1977, 99, 4860-4862.
17. (d) Shaked, Z.; Szajewski, R. P.; Whitesides, G. M. Biochemistry 1980, 19, 4156-4166.
18. (e) Houk, J.; Whitesides, G. M. J. Am. Chem. Soc. 1987, 109, 6825-6836.
19. (f) Keire, D. A.; Strauss, E.; Guo, W.; Noszal, B.; Rabenstein, D. L. J. Org. Chem. 1992, 57, 123-127.
20. (g) Rothwarf, D. M.; Scheraga, H. A. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 7944-7948.
21. (h) Fernandes, P. A.; Ramos, M. J. Chem.-Eur. J. 2004, 10, 257-266.
22. a (Table 1).
23. Evans, R. M.; Fraser, J. B.; Owen, L. N. J. Chem. Soc. 1947, 248-255.
24. The current price of DTT is 102-fold greater per thiol group than that of βME (Sigma-Aldrich, St. Louis, MO).
25. 2l
26. 2g Upon oxidation, however, BMS forms a seven-membered ring with E°′ = (-0.291 ± 0.002) V (Figure S3), making BMS a less potent reducing agent than DTT.
27. (a) Coppola, G. M.; Schuster, H. F. Asymmetric Synthesis: Construction of Chiral Molecules Using Amino Acids; John Wiley & Sons: New York, NY, 1987.
28. (b) McCaldon, P.; Argos, P. Proteins 1988, 4, 99-122.
29. Carbamate derivatives of DTBA are known. (a) Kessler, P.; Servent, D.; Hirth, C. Tetrahedron Lett. 1994, 35, 7237-7240.
30. (b) Servent, D.; Ménez, A.; Kessler, P. FEBS Lett. 1995, 360, 261-265.
31. Mitsunobu, O.; Masahiko, E. Bull. Chem. Soc. Jpn. 1971, 44, 3427-3430.
32. Jencks, W. P.; Salvesen, K. J. Am. Chem. Soc. 1971, 93, 4433-4436.
33. Connett, P. H.; Wetterhahn, K. E. J. Am. Chem. Soc. 1986, 108, 1842-1847.
34. Lees, W. J.; Whitesides, G. M. J. Org. Chem. 1993, 58, 642-647.
35. (a) Benesch, R. E.; Benesch, R. J. Am. Chem. Soc. 1955, 77, 5877-5881.
36. (b) Woycechowsky, K. J.; Wittrup, K. D.; Raines, R. T. Chem. Biol. 1999, 6, 871-879.
37. 13
38. Chivers, P. T.; Prehoda, K. E.; Raines, R. T. Biochemistry 1997, 36, 4061-4066.
39. (a) Roberts, D. D.; Lewis, S. D.; Ballou, D. P.; Olson, S. T.; Shafer, J. A. Biochemistry 1986, 25, 5595-5601.
40. (b) Singh, R.; Blattler, W. A.; Collinson, A. R. Anal. Biochem. 1993, 213, 49-56.
41. (a) Schechter, I.; Berger, A. Biochem. Biophys. Res. Commun. 1967, 27, 157-162.
42. (b) Pickersgill, R. W.; Harris, G. W.; Garman, E. Acta Crystallogr., Sect. B 1992, 48, 59-67.
43. Rao, J. K. M.; Bujacz, G.; Wlodawer, A. FEBS Lett. 1998, 439, 133-137.
44. (a) Putney, S.; Herlihy, W.; Royal, N.; Pang, H.; Aposhian, H. V.; Pickering, L.; Belagaje, R.; Biemann, K.; Page, D.; Kuby, S.; Schimmel, P. J. Biol. Chem. 1984, 259, 4317-4320.
45. (b) Chen, L. H.; Borders, C. L.; Vasquez, J. R.; Kenyon, G. L. Biochemistry 1996, 35, 7895-7902.
46. (c) Hurne, A. M.; Chai, C. L. L.; Waring, P. J. Biol. Chem. 2000, 275, 25202-25206.
47. (a) Amos, R. A.; Fawcett, S. M. J. Org. Chem. 1984, 49, 2637-2639.
48. (b) Woycechowsky, K. J.; Hook, B. A.; Raines, R. T. Biotechnol. Prog. 2003, 19, 1307-1314.
49. (c) Bienvenu, C.; Greiner, J.; Vierling, P.; Di Giorgio, C. Tetrahedron Lett. 2010, 51, 3309-3311.
50. Walker, J. M., Ed. The Protein Protocols Handbook, 3rd ed.; Humana Press: Totowa, NJ, 2009.