31P solid-state NMR measurements used to detect interactions between NADPH and water and to determine the ionisation state of NADPH in a protein-ligand complex subjected to low-level hydration

European Journal of Biochemistry

Volumn 235, Issue 1-2, 1996, Pages 262-266

  Gerothanassis, Ioannis P ^a   Barrie, Patrick J ^b   Birdsall, Berry ^c   Feeney, James ^c  

^a UNIVERSITY OF IOANNINA   (Greece)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

31P solid state NMR; Dihydrofolate reductase; Hydration; Magnetization transfer; NADPH

Indexed keywords

LACTOBACILLUS CASEI;

DIHYDROFOLATE REDUCTASE; ION; LIGAND; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN; WATER; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; LACTOBACILLUS CASEI; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; ENZYME BINDING; ENZYME STRUCTURE; HYDRATION; IONIZATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL;

BINDING SITES; IONS; LACTOBACILLUS CASEI; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR STRUCTURE; NADP; PROTEIN BINDING; PROTEINS; TETRAHYDROFOLATE DEHYDROGENASE; WATER;

EID: 0029671235     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00262.x     Document Type: Article

References (26)

1. Blakley, R. L. (1979) in Folates and pterins-chemistry and biochemistry of folates (Blakley, R. L. & Bencovic, S. J., eds) vol. 1, pp. 191-253, Wiley, New York.
2. Filman, D. J., Bolin, J. T., Matthews, D. A. & Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. J. Biol. Chem. 257, 13663-13672.
3. + binding to L. casei dihydrofolate reductase. Nature 257, 564-566.
4. + with E. coli dihydrofolate reductase. Int. J. Biol. Macromol. 2, 251-255.
5. 1H NMR saturation transfer studies of coenzyme binding to Lactobacillus casei dihydrofolate reductase, Biochemistry 19, 3738-3746.
6. 31P-NMR studies of the binding of oxidised coenzymes to L. casei dihydrofolate reductase, Biochemistry 19, 3746-3754.
7. Feeney, J. (1988) Studies of antifolate drugs binding to dihydrofolate reductase, Proc. Alfred Benzon Symp. 26, 173-190.
8. + and the complex of NADPH and methotrexate with Lactobacillus casei dihydrofolate reductase in the solid state, Eur. J. Biochem. 226, 211-218.
9. Dann, J. G., Ostler, G., Bjur, R. A., King, R. W., Scudder, P., Turner, P. C., Roberts, G. C. K. & Burgen, A. S. V. (1976) Large-scale purification and characterization of dihydrofolate reductase from a methotrexate-resistant strain of Lactobacillus casei, Biochem. J. 157, 559-571.
10. Herzfeld, J. & Berger, A. E. (1980) Side-band intensities in NMR spectra of sample spinning at the magic angle. J. Chem. Phys. 73, 6021-6030.
11. 13C NMR of iron carbonyl complexes: shielding tensor and error analysis, Proc. R. Soc. Lond. A 424, 93-111.
12. Harbison, G. S., Roberts, J. E., Herzfeld, J. & Griffin, R. G. (1988) Solid state NMR detection of proton exchange between Bacteriorhodopsin Schiff base and bulk water, J. Am. Chem. Soc. 110, 7221-7223.
13. Schaefer, J. & Stejskal, E. O. (1976) Carbon-13 nuclear magnetic resonance of polymers spinning at the magic angle, J. Am. Chem. Soc. 98, 1031-1032.
14. Volkin, D. B. & Klibanov, A. M. (1990) Minimizing protein inactivation, in Protein function: a practical approach (Creighton, T. E., ed.) pp. 1-24, IRL Press.
15. Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C. & Kraut, J. (1982) Crystal structures of E. coli and L. casei dihydrofolate reductase refined to 1.7 Å resolution. I. General features and binding of methotrexate, J. Biol. Chem. 257, 13650-13662.
16. Marchetti, P. S., Ellis, P. D. & Bryant, R. G. (1985) Cadmium-113 shielding tensors in cadmium substituted metalloproteins, J. Am. Chem. Soc. 107, 8191-8196.
17. 13C solids NMR, Biopolymers 29, 1801-1806.
18. 13C NMR spectroscopy, Biopolymers 33, 513-519.
19. 13C NMR spectroscopy, Biopolymers 33, 1871-1876.
20. Hemminga, M. A., DeJager, P. A., Krüse, J. & Lamerichs, R. M. J. N. (1982) Magic-angle spinning NMR on solid biological systems. Analysis of the origin of the spectral linewidths, J. Magn. Reson. 71, 446-460.
21. 31P shift correlation experiments, Eur, J. Biochem. 204, 173-177.
22. 31P NMR shielding in the pyrophosphate group of NADPH binding to L. casei dihydrofolate reductase, FEBS Lett. 291, 21-23.
23. Matthews, B. W. (1968) Solvent content of protein crystals, J. Mol. Biol. 33, 491-497.
24. Finer-Moore, J. S., Kossiakoff, A. A., Hurley, J. H., Earnest, T. & Stroud, R. M. (1992) Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction, Proteins 12, 203-222.
25. Wüthrich, K. (1986) NMR of proteins and nucleic acids, Wiley, New York.
26. Eichele, K. & Wasylishen, R. E. (1994) P-31 NMR. Study of powder and single crystal samples of ammonium dihydrogen phosphates - effects of homonuclear dipolar coupling, J. Phys. Chem. 98, 3108-3113.