4872 T3D4817 Riboflavin Nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. The richest natural source is yeast. It occurs in the free form only in the retina of the eye, in whey, and in urine; its principal forms in tissues and cells are as flavin mononucleotide and flavin-adenine dinucleotide. 83-88-5 493570 C17H20N4O6 White powder. 280 dec°C 84.7 mg/L (at 25°C) Vitamin B2 is readily absorbed from the upper gastrointestinal tract. Binds to riboflavin hydrogenase, riboflavin kinase, and riboflavin synthase. Riboflavin is the precursor of flavin mononucleotide (FMN, riboflavin monophosphate) and flavin adenine dinucleotide (FAD). The antioxidant activity of riboflavin is principally derived from its role as a precursor of FAD and the role of this cofactor in the production of the antioxidant reduced glutathione. Reduced glutathione is the cofactor of the selenium-containing glutathione peroxidases among other things. The glutathione peroxidases are major antioxidant enzymes. Reduced glutathione is generated by the FAD-containing enzyme glutathione reductase. Hepatic. Half Life: 66-84 minutes No indication of carcinogenicity to humans (not listed by IARC). For the treatment of ariboflavinosis (vitamin B2 deficiency). 2014-09-11T05:17:53Z 2026-03-27T01:46:13Z Riboflavin C00255 17015 RIBOFLAVIN DB00140 RBF true CC1=C(C)C=C2N(C[C@H](O)[C@H](O)[C@H](O)CO)C3=NC(=O)NC(=O)C3=NC2=C1 C17H20N4O6 InChI=1S/C17H20N4O6/c1-7-3-9-10(4-8(7)2)21(5-11(23)14(25)12(24)6-22)15-13(18-9)16(26)20-17(27)19-15/h3-4,11-12,14,22-25H,5-6H2,1-2H3,(H,20,26,27)/t11-,12+,14-/m0/s1 AUNGANRZJHBGPY-SCRDCRAPSA-N 376.3639 376.138284392 Endogenous Solid -1.46 HMDB00244 CHEMBL1534 6501 <p>Hansgeorg Ernst, Wolfram Schmidt, Joachim Paust, &#8220;Preparation of riboflavin.&#8221; U.S. Patent US4567261, issued August, 1958.</p> CHEM003774 DTXSID8021777 NS00007684 7,8-dimethyl-10-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-2H,3H,4H,10H-benzo[g]pteridine-2,4-dione