Following absorption riboflavin is converted into the co-enzymes: flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).

Following absorption riboflavin is converted into the coenzymes: flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).

The first polypeptide comprises an LOV (Light, Oxygen or Voltage) domain, which domain is a light sensor that uses flavin mononucleotide (FMN) as a chromophore.

One particular riboswitch, the flavine mononucleotide (FMN)-activated riboswitch, is a promising target for antibiotics.

In order to be able to utilize fluorescence reporters as markers for secretion processes, FMN-binding fluorescence proteins (FbFP) have been developed by us for the first time.

Glyphosate oxidoreductase is coupled to a cycling flavin mononucleotide-oxidoreductase-luciferase system.

Riboflavin is phosphorylated to flavin mononucleotide and flavin adenine dinucleotide which act as co-enzymes in the respiratory chain and in oxidative phosphorylation.

When expressed in a bacterial or mammalian cell, miniSOG proteins spontaneously incorporate flavin mononucleotide and produce fluorescence and singlet oxygen upon excitation.

Riboflavine is phosphorylated to flavine mononucleotide and flavine adenine dinucleotide which act as co-enzymes in the respiratory chain and in oxidative phosphorylation.