Search results
Results from the WOW.Com Content Network
Pathogen reduction using riboflavin and UV light is a method by which infectious pathogens in blood for transfusion are inactivated by adding riboflavin and irradiating with UV light. [ 1 ] [ 2 ] [ 3 ] This method reduces the infectious levels of disease-causing agents that may be found in donated blood components, while still maintaining good ...
Riboflavin, or vitamin B, and flavin mononucleotide are two of the most well known flavins in the body and are used in a variety of processes which include metabolism of fat [1] and ketones [2] and the reduction of methemoglobin in erythrocytes. [3]
This enzyme catalyses the reduction of soluble flavins. The structure of the protein suggests that the enzymatic mechanism of flavin reductase is of a bisubstrate-biproduct nature3. Due to its structural features, the enzyme is not able to bind both NAD(P)H and flavin at the same time.
The flavin group is capable of undergoing oxidation-reduction reactions, and can accept either one electron in a two-step process or two electrons at once. Reduction is made with the addition of hydrogen atoms to specific nitrogen atoms on the isoalloxazine ring system: Equilibrium between the oxidized (left) and totally reduced (right) forms ...
Riboflavin, also known as vitamin B 2, is a vitamin found in food and sold as a dietary supplement. [3] It is essential to the formation of two major coenzymes, ...
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B 2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors. [1]
Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes.
FAD plays a major role as an enzyme cofactor along with flavin mononucleotide, another molecule originating from riboflavin. [8] Bacteria, fungi and plants can produce riboflavin, but other eukaryotes, such as humans, have lost the ability to make it. [9] Therefore, humans must obtain riboflavin, also known as vitamin B2, from dietary sources. [14]