flaviniiniadeniinidinukleotidi

Flaviniiniadeniinidinukleotidi, commonly known as FAD, is a vital coenzyme found in all living organisms. It is a redox cofactor that participates in numerous metabolic reactions. Chemically, FAD is composed of two key components: adenosine diphosphate (ADP) and flavin mononucleotide (FMN). The flavin moiety, specifically the isoalloxazine ring system within FMN, is responsible for FAD's ability to accept and donate electrons. This reversible redox activity is central to its biological function.

FAD plays a crucial role in cellular respiration, acting as an electron carrier in various enzyme-catalyzed reactions, particularly in the citric acid cycle and the electron transport chain. It is the prosthetic group for a large class of enzymes called flavoproteins, which include oxidases, reductases, and dehydrogenases. These enzymes catalyze a wide array of metabolic transformations, such as the oxidation of fatty acids and amino acids, as well as the reduction of molecular oxygen. The reduction of FAD to FADH2 involves the addition of two protons and two electrons to the isoalloxazine ring. Subsequently, FADH2 can donate these electrons to other molecules, regenerating FAD for further catalytic cycles. Beyond energy metabolism, FAD is also involved in DNA repair and the synthesis of certain vitamins. Its essential nature makes it a ubiquitous and indispensable molecule in biochemistry.