Description
Flavin Adenine Dinucleotide Disodium Salt hydrate is an adenine-containing enzymatic redox cofactor. Also known as flavin cofactors and is critical electron transporter in living systems. FAD has been used as a predominant fluorophore to study unstained eosinophils, which exhibit autofluorescence compared to other leucocytes.
Chemical Properties
yellow-orange powder
Uses
The prosthetic group of certain flavoproteins including D-amino acid oxidase, glucose oxidase, glycine oxidase, fumaric hydrogenase, histaminase, and xanthine oxidase. Riboflavin kinase tumor necrosis factor receptor 1 NADPH oxidase.
Uses
Used as a redox cofactor (electron carrier) for flavoproteins including succinate dehydrogenase (complex), alpha-ketoglutarate dehydrogenase, apoptosis-inducing factor 2 (AIF-M2) , AMID), folate/FAD-dependent tRNA methyltransferase, and N-hydroxylated flavoprotein monooxygenase.
Application
Flavin adenine dinucleotide disodium salt is the sodium salt form of Flavin adenine dinucleotide (FAD). FAD is used by flavoproteins as redox cofactors (electron carriers), including succinate dehydrogenase (complex), α-ketoglutarate dehydrogenase, apoptosis inducing factor 2 (AIF-M2, AMID), folate/FAD-dependent tRNA methyltransferase, and N-hydroxylated flavoprotein monooxygenase. FAD is a component of the pyruvate dehydrogenase complex. Flavin adenine dinucleotide disodium salt hydrate has been used as a component of plant tissue extraction buffers.
Definition
ChEBI: Flavin adenine dinucleotide disodium is a flavin nucleotide.
Origin
Flavin adenine dinucleotide (FAD) disodium salt is derived from vitamin B2. It is an active, water-soluble coenzyme form of vitamin B2 (riboflavin) and acts as an essential electron carrier in cellular metabolism.
Biological Activity
Flavin adenine dinucleotide (FAD) disodium salt is a redox cofactor, a prosthetic group of proteins, involved in several important enzymatic reactions during metabolism.
in vitro
Poly(Flavin adenine dinucleotide, FAD) characterized by an additional polymer-type redox reaction is a highly effective electrocatalyst for NADH oxidation: operating at the lowest potentials reported for NADH transducers (0.00 V, pH 7.4), poly(FAD) is characterized by the electrochemical rate constant of 1.8 ± 0.6×10 -3 cm/s, which is at the level of the NADH mass-transfer constant. Poly(FAD)-modified electrodes are characterized by the dramatically improved stability and, is the most advantageous NADH transducers for analytical chemistry.
in vivo
With Flavin adenine dinucleotide (2 mg/kg), the chlorpromazine (CPZ)-induced decrease in ventricular fibrillation threshold (VFT) is significantly cancelled. Flavin adenine dinucleotide cancels the effect of CPZ on canine heart mitochondria. After injection of Flavin adenine dinucleotide, the dogs show a transient hypotension within 10 min, then their blood pressures recover to the initial level. Flavin adenine dinucleotide also prevents mitochondrial dysfunction induced by chlorpromazine.
Purification Methods
Small quantities of FAD are purified by paper chromatography using tert-butyl alcohol/water, cutting out the main spot and eluting with water. Larger amounts can be precipitated from water as the uranyl complex by adding a slight excess of uranyl acetate to a solution at pH 6.0, dropwise and with gentle stirring. The solution is set aside overnight in the cold, and the precipitate is centrifuged off, washed with small portions of cold EtOH, then with cold peroxide-free diethyl ether. It is dried in the dark under vacuum over P2O5 at 50-60o. The uranyl complex is suspended in water, and, after adding sufficient 0.01M NaOH to adjust the pH to 7, the precipitate of uranyl hydroxide is removed by centrifugation [Huennekens & Felton Methods Enzymol 3 954 1957]. It can also be crystallised from water. It should be kept in the dark. More recently it was purified by elution from a DEAE-cellulose (Whatman DE 23) column with 0.1M phosphate buffer pH 7, and the purity was checked by TLC. [Holt & Cotton, J Am Chem Soc 109 1841 1987, Beilstein 26 III/IV 3632.]
