Exploring the limits of efficiency of proton-transfer catalysis in models and enzymes [16]

Journal of the American Chemical Society

Volumn 122, Issue 38, 2000, Pages 9326-9327

  Hartwell, Ewa ^a   Hodgson, David R W ^a   Kirby, Anthony J ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; PROTON;

CATALYSIS; CHEMICAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME KINETICS; HYDROGEN BOND; HYDROLYSIS; LETTER; MOLECULAR INTERACTION; PH; PRODUCTIVITY; PROTON TRANSPORT;

EID: 0034721416     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja002335m     Document Type: Letter

References (24)

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2. Richard, J. P. Biochemistry 1998, 37, 4305-9.
3. The EM is defined as the concentration of a catalytic group, in a separate molecule, required to make the corresponding intermolecular reaction go as fast as the intramolecular reaction of interest. Kirby, A. J. Adv. Phys. Org. Chem. 1980, 17, 183-278.
4. Kirby, A. J.; Parkinson, A. J. Chem. Soc., Chem. Commun. 1994, 707-8.
5. Brown, C. J.; Kirby, A. J. J. Chem. Soc., Perkin Trans. 2 1997, 1081-1093.
6. -1 for the rate constant for hydrolysis at 39 °C of 1 lacking the carboxyl group.
7. -1 at 60 °C) as that obtained from the measurements of Wolfenden et al. 11
8. Craze, G.-A.; Kirby, A. J. J. Chem. Soc., Perkin Trans. 2 1978, 354-6.
9. Cordes, E. H.; Bull, H. G. Chem. Rev. 1974, 74, 581-603.
10. Craze, G.-A.; Kirby, A. J.; Osborne, R. J. Chem. Soc., Perkin Trans. 2 1978, 357-368.
11. Wolfenden, R.; Lu, X.; Young, G. J. Am. Chem. Soc. 1998, 120, 6814-6815.
12. Nath, R. L.; Rydon, H. N. Biochem. J. 1954, 57, 1-9.
13. 10 mL of a stock solution of 4 in methanol (5 mg/mL) was added to 0.01 M aqueous buffer (190 μL) of ionic strength 0.05 M (KCl), containing 4-nitrobenzenesulfonate as integration standard. Two 70 μL aliquots were sealed in ampules and incubated in a water bath at 39 °C, and the remaining solution retained as a control. Sealed ampules were removed at intervals, cooled, and opened and 20 μL aliquots were added to 0.2 M KOH (5 μL) to stop the reaction. Both samples and the control were analyzed by capillary electrophoresis using a Beckmann-Coulter PACE MDQ instrument (at 264 nm, 25 °C, run buffer 0.1M phosphate, pH 6.20).
14. Craze, G.-A.; Kirby, A. J. J. Chem. Soc., Perkin Trans. 2 1974, 61.
15. Fife, T. H.; Przystas, T. J. J. Am. Chem. Soc. 1979, 101, 1202-1210.
16. Hibbert, F.; Emsley, J. Adv. Phys. Org. Chem. 1990, 26, 255-379.
17. Gerlt, J. A.; Gassman, P. G. J. Am. Chem. Soc. 1993, 115, 11552-11568.
18. Gerlt, J. A.; Kreevoy, M. M.; Cleland, W. W.; Frey, P. A. Chem. Biol. 1997, 4, 259-267.
19. Guthrie, J. P.; Kluger, R. J. Am. Chem. Soc. 1993, 115, 11569-11572.
20. Guthrie, J. P. Chem. Biol. 1996, 3, 163-170.
21. Chen, J. G.; McAllister, M. A.; Lee, J. K.; Houk, K. N. J. Org. Chem. 1998, 65, 4611-4619.
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23. Barber, S. E.; Dean, K. E. S.; Kirby, A. J. Can. J. Chem. 1999, 792-801.
24. The problem has been discussed in detail in a recent review: Schowen, K. B.; Limbach, H. H.; Denisov, G. S.; Schowen, R. L. Biochim. Biophys. Acta Bioenerg. 2000, 1458, 43-62.