The first mention of a flavoprotein in the scientific literature dates back to 1879, when the work on the composition of cow’s milk resulted in the isolation of a bright-yellow pigment, that we now know as flavin, but termed lactochrome at the time.
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The spectroscopic properties of the flavin cofactor make it a natural reporter for changes occurring within the active site; this makes flavoproteins one of the most-studied enzyme families.
In fact, one of the proteins involved in the oxidative folding process uses a flavin-dependent reaction to pass electrons directly to molecular oxygen.
Pterins and flavins are classes of substituted pteridines that have important biological activity.
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