Hydrogen bonding effects on 31P NMR shielding in the pyrophosphate group of NADPH bound to L. casei dihydrofolate reductase

A comparison of 31P NMR chemical shift data and X-ray structural data [Filman, D.J., Bolin, J.T., Matthews, D.A. and Kraut, J. (1982) J. Biol. Chem. 257, 13663–13672] for complexes of NADPH with L. casei dihydrofolate reductase indicates that solvation effects play a major role in influencing the 31...

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Veröffentlicht in:	FEBS letters 1991-10, Vol.291 (1), p.21-23
Hauptverfasser:	Gerothanassis, I.P., Birdsall, B., Feeney, J.
Format:	Artikel
Sprache:	eng
Schlagworte:	31P NMR Biological and medical sciences Cell physiology DHFR Diphosphates - chemistry Fundamental and applied biological sciences. Psychology Hydrogen Bonding Lactobacillus casei - enzymology Magnetic Resonance Spectroscopy Molecular and cellular biology NADP - chemistry NADP - metabolism NADPH Solvation Tetrahydrofolate Dehydrogenase - chemistry Tetrahydrofolate Dehydrogenase - metabolism X-Ray Diffraction
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Zusammenfassung:	A comparison of 31P NMR chemical shift data and X-ray structural data [Filman, D.J., Bolin, J.T., Matthews, D.A. and Kraut, J. (1982) J. Biol. Chem. 257, 13663–13672] for complexes of NADPH with L. casei dihydrofolate reductase indicates that solvation effects play a major role in influencing the 31P shielding of the pyrophosphate nuclei whereas changes in P-O-C 5-H 5' torsion angle have little effect.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(91)81094-O