4091. Flavine-Adenine Dinucleotide

Nomenclature

CAS number: 146-14-5
Riboflavine 5′-(trihydrogen diphosphate) 5′→5′-ester with adenosine; adenosine 5′-(trihydrogen diphosphate) 5′→5′-ester with riboflavine; FAD; riboflavine 5′-adenosine diphosphate; isoalloxazine-adenine dinucleotide; Fademin (Chugai); Flamitajin (Teisan; Iwaki); Flanin F (Tokyo Tanabe); Flavitan.
C27H33N9O15P2; mol wt 785.55.
C 41.28%, H 4.23%, N 16.05%, O 30.55%, P 7.89%.

Description and references

The prosthetic group of certain flavoproteins including d-amino acid oxidase, glucose oxidase, glycine oxidase, fumaric hydrogenase, histaminase, and xanthine oxidase. Isoln from yeast: Warburg et al., Biochem. Z. 297, 417 (1938). Structure and isoln from liver, kidneys, hearts, muscles: Warburg, Christian, ibid. 298, 150 (1938); isoln from the mycelium of Eremothecium ashbyii: Yagi, Tada, Biochem. Prep. 7, 51 (1959); Masuda et al., US 2973305 (1961 to Takeda). Synthesis: Christie et al., J. Chem. Soc. 1954, 46; Huennekens, Kilgour, J. Am. Chem. Soc. 77, 6716 (1955); DeLuca, Kaplan, J. Biol. Chem. 223, 569 (1956); Moffatt, Khorana, J. Am. Chem. Soc. 80, 3756 (1958). Review: A. Holmgren, Experientia 36 (Suppl), 149-180 (1980). Review of FAD and other flavin coenzymes: Beinert, The Enzymes vol. 2, P. D. Boyer et al., Eds. (Academic Press, New York, 2nd ed., 1960) pp 339-416; see also vol. XIII Part B (Academic Press, New York, 3rd ed., 1975), several authors.

Chemical structure

Derivative

Barium salt.
C27H31BaN9O15P2; mol wt 920.86.
C 35.22%, H 3.39%, Ba 14.91%, N 13.69%, O 26.06%, P 6.73%.

Properties

Small yellow spheres clustered like grapes. Absorption max: 366, 445 nm. The absorption curve is practically identical with that of riboflavine. There is some stronger absorption between 450 and 510 nm resulting in aq solns which are more reddish and less green than those of riboflavine. The appearance of a strong greenish fluorescence indicates decomposition and loss of catalytic activity.