1H NMR spectral analysis of the ribityl side chain of riboflavin and its ring-substituted analogs☆
Review articleOpen access
1986/01/01 Full-length article DOI: 10.1016/0076-6879(86)22177-1
Publisher SummaryThis chapter presents 1H NMR spectral analysis of the ribityl side chain of riboflavin and its ring-substituted analogs. It describes the results of these analyses using several riboflavin analogs in D2O solutions at various pH values as demanded for solubilization of the analog of interest. Confirmation of spectral assignments is also illustrated by selectively monodeuterating the 5′-CH2 group of the riboflavin side chain. The 1H NMR spectra of the ribityl side chain could be useful for structural studies of flavin coenzymes which appear to have alterations in the ribityl side chain. 1H NMR spectral simulations are performed using the NMCSIM program on the computer of the Nicolet spectrometer. All 1H NMR spectra are acquired using a Nicolet 360 MHz spectrometer in 5-mm NMR tubes at ambient temperature. A sweep width of 4000 Hz is used with 16,000 data points. These NMR spectral analyses might profitably be applied to the phosphorylated coenzyme forms of riboflavin—namely, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).
Request full text