Hydride transfer versus hydrogen radical transfer in thymidylate synthase

Journal of the American Chemical Society

Volumn 128, Issue 17, 2006, Pages 5636-5637

  Hong, Baoyu ^a   Haddad, Majd ^a   Maley, Frank ^b   Jensen, Jan H ^a   Kohen, Amnon ^a  

^a E11 SSH   (United States)

^b WADSWORTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DEOXYURIDINE PHOSPHATE; DNA; FOLIC ACID; HYDROGEN; PHENYLALANINE; RADICAL; THYMIDINE PHOSPHATE; THYMIDYLATE SYNTHASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL REACTION; CRYSTAL STRUCTURE; ENERGY; ENZYME ACTIVITY; KINETICS; PROTON TRANSPORT; TEMPERATURE DEPENDENCE;

HYDROGEN; THYMIDYLATE SYNTHASE;

EID: 33646538128     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja060196o     Document Type: Article

References (35)

1. Carreras, C. W.; Santi, D. V. Annu. Rev. Biochem. 1995, 64, 721-762.
2. Stroud, R. M.; Finer-Moore, J. S. Biochemistry 2003, 42, 239-247 and references cited therein.
3. Finer-Moore, J. S.; Santi, D. V.; Stroud, R. M. Biochemistry 2003, 42, 248-256 and references cited therein.
4. Barrett, J. E.; Maltby, D. A.; Santi, D. V.; Schultz, P. G. J. Am. Chem. Soc. 1998, 120, 449-450.
5. Barren, J. E.; Lucero, C. M.; Schultz, P. G. J. Am. Chem. Soc. 1999, 121, 7965-7966.
6. The L. casei TS (lcTS) W82 is equivalent to the E. coli TS (ecTS) W80. In the past, most structural studies were conducted with ecTS, while most kinetic studies used lcTS, but both are commonly treated as equivalent and comparable isozymes.
7. Fritz, T. A.; Liu, L.; Finer-Moore, J. S.; Stroud, R. M. Biochemistry 2002, 41, 7021-7029.
8. Meaning the H-transfer step reaction's potential surface, dynamics, adiabatic reaction or non-adiabatic reaction, hydride or radical transfer, and other physical features of the C-H-C double well system that will affect the KIEs and their temperature dependence as discussed in refs 10-13.
9. KIE is the ratio of rates of two isotopically labeled reactants.
10. Agrawal, N.; Hong, B.; Mihai, C.; Kohen, A. Biochemistry 2004, 43, 1998-2006.
11. Hammes-Schiffer, S. (Chapter 19);
12. Kiefer, P. M.; Hynes, J. T. (Chapter 21);
13. Truhlar, D. G. (Chapter 22),
14. 23 by Warshel, A.; et al. (Chapter 23);
15. Kuznetsov, A. M.; Ulstrup, J. (Chapter 26)
16. In Isotope Effects in Chemistry and Biology, Kohen, A., Limbach, H. H., Eds.; Taylor & Francis, CRC Press: Boca Raton. FL, 2006.
17. Knapp, M. J.; Rickert, K.; Klinman, J. P. J. Am. Chem. Soc. 2002, 124, 3865-3874.
18. Hammes-Schiffer, S. Acc. Chem. Res. 2006, 39, 93-100.
19. Kohen, A.; Cannio, R.; Bartolucci, S.; Klinman, J. P. Nature 1999, 399. 496-499.
20. Rickert, K. W.; Klinman, J. P. Biochemistry 1999, 38, 12218-12228.
21. Wang, L.; Tharp, S.; Selzer, T.; Benkovic, S. J.; Kohen, A. Biochemistry 2006, 45, 1383-1392.
22. Wang, L.; Goodey, N. M.; Benkovic, S. J.; Kohen, A. Philos. Trans. R, Soc. London, Ser. B 2006, in press.
23. Basran, J.; et al. (Chapter 25);
24. Kohen, A. (Chapter 28)
25. In Isotope Effects in Chemistry and Biology; Kohen, A., Limbach, H. H., Eds.; Taylor & Francis. CRC Press: Boca Raton, FL, 2006.
26. Kealey, J. T.; Eckstein, J.; Santi, D. V. Chem. Biol. 1995, 2, 609-614.
27. See Supporting Information.
28. Ma, J. C.; Dougherty, D. A. Chem. Rev. 1997, 97, 1303-1324.
29. This value is actually a underestimation of the differences between M and W. The level of theory used by Schultz and us (RHF/6-31G(d,p)//RHF/6-31G(d,p)) following the footsteps of refs 5 and 21 do not include the additional stabilization anticipated form the π-stacking interactions between the pterin and the indole aromatic rings.
30. Agrawal, N.; Mihai, C.; Kohen, A. Anal. Biochem. 2004, 328, 44-50.
31. Cleland, W. W. In Isotope Effects in Chemistry and Biology; Kohen, A., Limbach, H. H., Eds.; Taylor & Francis, CRC Press: Boca Raton, FL, 2006; Chapter 37, pp 915-930.
32. Swain, C. G.; Stivers, E. C.; Reuwer, J. F.; Schaad, L. J. J. Am. Chem. Soc. 1958, 80, 5885-5893.
33. Bahnson, B. J.; Klinman, J. P. Methods Enzymol. 1995, 249, 373-397.
34. Northrop, D. B. In Enzyme Mechanism from Isotope Effects: Cook, P. F., Ed.; CRC Press: Boca Raton, FL, 1991; pp 181-202.
35. The errors of the M80W K1Es are much smaller than those for the wt because W80M's observed K1E equal to the intrinsic ones and no error propagation through Northrop's numerical solution is necessary (for details of that error propagation and regression procedures, see ref 16).