pH-dependent conformational changes in Escherichia coli dihydrofolate reductase revealed by raman difference spectroscopy

Biophysical Journal

Volumn 72, Issue 2 I, 1997, Pages 936-941

  Chen, Yong Qing ^a,b   Kraut, Joseph ^b   Callender, Robert ^a,c,d  

^a CITY COLLEGE OF NEW YORK   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CITY UNIVERSITY OF NEW YORK   (United States)

^d ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ESCHERICHIA COLI; NONHUMAN; PH; RAMAN SPECTROMETRY; STRUCTURE ACTIVITY RELATION;

EID: 0031030973     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78727-7     Document Type: Article

References (25)

1. Adams, J., K. Johnson, R. Matthews, and S. J. Benkovic. 1989. Effects of distal point-site mutations on the binding and catalysis of dihydrofolate reductase from Escherichia coli. Biochemistry. 28:6611-6618.
2. Appleman, J. R., E. E. Howell, J. Kraut, and R. L. Blakley. 1990. Role of aspartate-27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH. J. Biol. Chem. 265:5579-5584.
3. Basran, J., M. G. Casarotto, I. L. Barsukov, and G. C. K. Roberts. 1995. Role of the active-site carboxylate in dihydrofolate reductase - kinetic and spectroscopic studies of the aspartate 26 to asparagine mutant of the Lactobacillus casei enzyme. Biochemistry. 34:2872-2882.
4. 15N nuclear magnetic resonance evidence that the active site carboxyl group of dihydrofolate reductase is not involved in the relay of a proton to substrate. Arch. Biochem. Biophys. 306:501-509.
5. Bolin, J. T., D. J. Filman, D. A. Matthews, R. C. Hamlin, and J. Kraut. 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 ≈ resolution I. General features and binding of methotrexate. J. Biol. Chem. 257:13650-13662.
6. Bystroff, C., and J. Kraut. 1991. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry. 30:2227-2239.
7. + ternary complex. Substrate binding and a model for the transition state. Biochemistry. 29:3263-3277.
8. Callender, R., and H. Deng. 1994. Nonresonance raman difference spectroscopy - a general probe of protein structure, ligand binding, enzymatic catalysis, and the structures of other biomacromolecules. Annu. Rev. Biophys. Biomol. Struct. 23:215-245.
9. Chen, Y.-Q., J. Kraut, R. L. Blakley, and R. Callender. 1994. Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to Escherichia coli dihydrofolate reductase - mechanistic implications. Biochemistry. 33:7021-7026.
10. Daimay, L.-V., N. B. Colthup, W. G. Fateley, and J. G. Grasselli. 1991. The Handbook of Infrared and Raman Characteristic Frequencies of Organic Molecules. Academic Press, San Diego, CA.
11. Dioumaev, A. K., and M. S. Braiman. 1995. Modeling vibrational spectra of amino acid side chains in proteins - the carbonyl stretch frequency of buried carboxylic residues. J. Am. Chem. Soc. 117:10572-10574.
12. Falzone, C. J., P. E. Wright, and S. J. Benkovic. 1994. Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implications for catalysis. Biochemistry. 33:439-442.
13. Fierke, C. A., K. A. Johnson, and S. J. Benkovic. 1987. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry. 26:4085-4092.
14. Howell, E. E., J. E. Villafranca, M. S. Warren, S. J. Oatley, and J. Kraut. 1986. Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. Science. 231:1123-1128.
15. Howell, E. E., M. S. Warren, C. L. J. Booth, J. E. Villafranca, and J. Kraut. 1987. Construction of an altered proton donation mechanism in Escherichia coli dihydrofolate reductase. Biochemistry. 26:8591-8598.
16. Huennekens, F. M., and K. G. Scrimgeour. 1964. Tetrahydrofolic acid - the coenzyme of one-carbon metabolism. In Pteridine Chemistry (W. Pfliederer and E. C. Taylor, editors. MacMillan, Oxford, England. 355-376.
17. Li, L., and S. J. Benkovic. 1991. Impact on catalysis of secondary structural manipulation of the αC-helix of Escherichia coli dihydrofolate reductase. Biochemistry. 30:1470-1478.
18. Maruyama, T., and H. Takeuchi. 1995. Effects of hydrogen bonding and side-chain conformation on the Raman bands of tryptophan-,4,5,6,7-d5. J. Raman Spectrosc. 26:319-324.
19. Miura, T., H. Takeuchi, and I. Harada. 1989. Tryptophan Raman bands sensitive to hydrogen bonding and side-chain conformation. J. Raman Spectrosc. 20:667-671.
20. Morrison, J. F., and S. R. Stone. 1988. Mechanism of the reaction catalysed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrate. Biochemistry. 27:5499-5506.
21. Stone, S. R., and J. F. Morrison. 1983. The pH-dependence of the binding of dihydrofolate and substrate analogues to dihydrofolate reductase from Escherichia coli. Biochim. Biophys. Acta. 745:247-258.
22. Stone, S. R., and J. F. Morrison. 1984. Catalytic mechanism of the dihydrofolate reductase reaction as determined by pH studies. Biochemistry. 23:2753-2758.
23. Takeuchi, H., and I. Harada. 1986. Normal coordinate analysis of indole ring. Spectrochim Acta A. 42:1069-1078.
24. Uchimaru, T., S. Tsuzuki, K. Tanabe, S. J. Benkovic, K. Furukawa, and K. Taira. 1989. Computational studies on pterins and speculations on the mechanism of action of dihydrofolate reductase. Biochim. Biophys. Res. Commun. 161:64-68.
25. Villafranca, J. E., E. E. Howell, D. H. Voet, M. S. Strobel, R. C. Ogden, J. N. Abelson, and J. Kraut. 1983. Directed mutagenesis of dihydrofolate reductase. Science. 222:782-788.