A <sup>13</sup>C Nuclear‐Magnetic‐Resonance Study of the Enzyme Cofactor Flavin‐Adenine Dinucleotide

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<jats:p>An assignment of the <jats:sup>13</jats:sup>C‐NMR spectrum of the enzyme cofactor flavin‐adenine dinucleotide (FAD) is given by comparing it with the <jats:sup>13</jats:sup>C chemical shifts of the constituents of FAD, <jats:italic>i.e.</jats:italic> adenosine 5′‐diphosphate, riboflavin 5′‐monophosphate, riboflavin, adenosine and adenine. The <jats:sup>13</jats:sup>C‐NMR spectrum of FAD shows three groups of signals:</jats:p><jats:p>a) At highest field the resonances of the methyl groups (‐18 to ‐21 ppm) of the isoalloxazine moiety.</jats:p><jats:p>b) At lowest field the signals of the carbon atoms of the isoalloxazine ring (‐117 to ‐161 ppm).</jats:p><jats:p>c) In the range of ‐47 to ‐88 ppm the resonances of the carbon atoms of the ribose and ribitol residue.</jats:p>

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