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== History ==
[[Flavoproteins]] were first discovered in 1879 by separating components of cow's milk. They were initially called lactochrome due to their milky origin and yellow [[pigment]]. It took 50 years for the scientific community to make any substantial progress in identifying the molecules responsible for the yellow pigment. The 1930s launched the field of [[coenzyme]] research with the publication of many [[flavin group|flavin]] and [[nicotinamide]] derivative structures and their obligate roles in redox catalysis. German scientists [[Otto Heinrich Warburg|Otto Warburg]] and Walter Christian discovered a yeast derived yellow [[protein]] required for [[cellular respiration]] in 1932. Their colleague [[Hugo Theorell]] separated this yellow enzyme into [[apoenzyme]] and yellow pigment, and showed that neither the enzyme nor the pigment was capable of [[oxidizing]] [[NADH]] on their own, but mixing them together would restore activity. Theorell confirmed the pigment to be [[riboflavin]]'s phosphate ester, [[flavin mononucleotide]] (FMN) in 1937, which was the first direct evidence for [[enzyme]] [[Cofactor (biochemistry)|cofactors]]. Warburg and Christian then found FAD to be a cofactor of [[D-amino acid oxidase]] through similar experiments in 1938. Warburg's work with linking nicotinamide to hydride transfers and the discovery of flavins paved the way for many scientists in the 40s and 50s to discover copious amounts of redox biochemistry and link them together in pathways such as the [[citric acid cycle]] and [[Adenosine triphosphate|ATP]] synthesis.

Translations:Flavin adenine dinucleotide/4/en - Revision history

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