Flavin adenine dinucleotide consists of two main portions: an adenine nucleotide (adenosine monophosphate) and a flavin mononucleotide bridged together through their phosphate groups.
Adenine is bound to a cyclic ribose at the 1' carbon, while phosphate is bound to the ribose at the 5' carbon to form the adenine nucledotide.
Riboflavin is formed by a carbon-nitrogen (C-N) bond between an isoalloxazine and a ribitol.
The phosphate group is then bound to the on the terminal ribose carbon to form a FMN.
Because the bond between the isoalloxazine and the ribitol is not considered to be a glycosidic bond, the flavin mononucleotide is not truly a nucleotide.
This makes the dinucleotide name misleading; however, the flavin mononucleotide group is still very close to a nucleotide in its structure and chemical properties.

 
FAD can be reduced to FADH₂ through the addition of 2 H⁺ and 2 e⁻. FADH₂ can also be oxidized by the loss of 1 H⁺ and 1 e⁻ to form FADH.
The FAD form can be recreated through the further loss of 1 H⁺ and 1 e⁻. FAD formation can also occur through the reduction and dehydration of flavin-N(5)-oxide.
Based on the oxidation state, flavins take specific colors when in aqueous solution.
 flavin-N(5)-oxide (superoxidized) is yellow-orange, FAD (fully oxidized) is yellow, FADH (half reduced) is either blue or red based on the pH, and the fully reduced form is colorless.
Changing the form can have a large impact on other chemical properties.
For example, FAD, the fully oxidized form is subject to nucleophilic attack, the fully reduced form,  FADH₂ has high polarizability, while the half reduced form is unstable in aqueous solution.
FAD is an aromatic ring system, whereas FADH₂ is not.
This means that FADH₂ is significantly higher in energy, without the stabilization through resonance that the aromatic structure provides.
 FADH₂ is an energy-carrying molecule, because, once oxidized it regains aromaticity and releases the energy represented by this stabilization.

The spectroscopic properties of FAD and its variants allows for reaction monitoring by use of UV-VIS absorption and fluorescence spectroscopies.
Each form of FAD has distinct absorbance spectra, making for easy observation of changes in oxidation state.
A major local absorbance maximum for FAD is observed at 450 nm, with an extinction coefficient of 11,300.
Flavins in general have fluorescent activity when unbound (proteins bound to flavin nucleic acid derivatives are called flavoproteins).
This property can be utilized when examining protein binding, observing loss of fluorescent activity when put into the bound state.
Oxidized flavins have high absorbances of about 450 nm, and fluoresce at about 515-520 nm.
Flavin adenine dinucleotide consists of two main portions: an adenine nucleotide (adenosine monophosphate) and a flavin mononucleotide bridged together through their phosphate groups. Adenine is bound to a cyclic ribose at the 1' carbon, while phosphate is bound to the ribose at the 5' carbon to form the adenine nucledotide. Riboflavin is formed by a carbon-nitrogen (C-N) bond between an isoalloxazine and a ribitol. The phosphate group is then bound to the on the terminal ribose carbon to form a FMN. Because the bond between the isoalloxazine and the ribitol is not considered to be a glycosidic bond, the flavin mononucleotide is not truly a nucleotide. This makes the dinucleotide name misleading; however, the flavin mononucleotide group is still very close to a nucleotide in its structure and chemical properties. 
 
FAD can be reduced to FADH₂ through the addition of 2 H⁺ and 2 e⁻. FADH₂ can also be oxidized by the loss of 1 H⁺ and 1 e⁻ to form FADH. The FAD form can be recreated through the further loss of 1 H⁺ and 1 e⁻. FAD formation can also occur through the reduction and dehydration of flavin-N(5)-oxide. Based on the oxidation state, flavins take specific colors when in aqueous solution.  flavin-N(5)-oxide (superoxidized) is yellow-orange, FAD (fully oxidized) is yellow, FADH (half reduced) is either blue or red based on the pH, and the fully reduced form is colorless. Changing the form can have a large impact on other chemical properties. For example, FAD, the fully oxidized form is subject to nucleophilic attack, the fully reduced form,  FADH₂ has high polarizability, while the half reduced form is unstable in aqueous solution. FAD is an aromatic ring system, whereas FADH₂ is not. This means that FADH₂ is significantly higher in energy, without the stabilization through resonance that the aromatic structure provides.  FADH₂ is an energy-carrying molecule, because, once oxidized it regains aromaticity and releases the energy represented by this stabilization.
The spectroscopic properties of FAD and its variants allows for reaction monitoring by use of UV-VIS absorption and fluorescence spectroscopies. Each form of FAD has distinct absorbance spectra, making for easy observation of changes in oxidation state. A major local absorbance maximum for FAD is observed at 450 nm, with an extinction coefficient of 11,300. Flavins in general have fluorescent activity when unbound (proteins bound to flavin nucleic acid derivatives are called flavoproteins). This property can be utilized when examining protein binding, observing loss of fluorescent activity when put into the bound state. Oxidized flavins have high absorbances of about 450 nm, and fluoresce at about 515-520 nm.
Flavin adenine dinucleotide