Abstract
The 31P NMR spectra of NADPH and NADP+ in their complexes with dihydrofolate reductase show effects from three-bond 1H-31P coupling constants which indicate that the conformation about one of the C5′–O5′ bonds changes when the coenzyme is bound to the enzyme. 31P chemical shifts demonstrate that the 2′-phosphate group is in the dianionic state in the complex.
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Feeney, J., Birdsall, B., Roberts, G. et al. 31P NMR studies of NADPH and NADP+ binding to L. casei dihydrofolate reductase. Nature 257, 564–566 (1975). https://doi.org/10.1038/257564a0
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DOI: https://doi.org/10.1038/257564a0
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