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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]
The SI unit of molar absorption coefficient is the square metre per mole (m 2 /mol), but in practice, quantities are usually expressed in terms of M −1 ⋅cm −1 or L⋅mol −1 ⋅cm −1 (the latter two units are both equal to 0.1 m 2 /mol).
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]
absorption coefficient is essentially (but not quite always) synonymous with attenuation coefficient; see attenuation coefficient for details; molar absorption coefficient or molar extinction coefficient , also called molar absorptivity , is the attenuation coefficient divided by molarity (and usually multiplied by ln(10), i.e., decadic); see ...
Riboflavin, also known as vitamin B 2, is a water-soluble vitamin and is one of the B vitamins. [3] [4] [5] Unlike folate and vitamin B 6, which occur in several chemically related forms known as vitamers, riboflavin is only one chemical compound.
The absorption coefficient can, in turn, be written as a product of either a molar absorptivity of the absorber, ε, and the concentration c of absorbing species in the material, or an absorption cross section, σ, and the (number) density N of absorbers. (see Beer Lambert Law link for full derivation)
The anionic bound form of the dye which is held together by hydrophobic and ionic interactions, has an absorption spectrum maximum historically held to be at 595 nm. [5] The increase of absorbance at 595 nm is proportional to the amount of bound dye, and thus to the amount (concentration) of protein present in the sample.
The absorption spectrum of water in the range from 250 to 1000 nm is shown in Figure 2. Although absorption is rather low in this spectral range, it still contributes to the overall attenuation of tissue. Figure 3: The molar extinction coefficients of eumelanin and pheomelanin. [5]