Flavin mononucleotide

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Flavin Mononucleotide[edit | edit source]

Flavin mononucleotide (FMN) is a biomolecule that plays a crucial role in various biological processes. It is derived from riboflavin (vitamin B2) and serves as a cofactor for numerous enzymes involved in redox reactions.

Structure[edit | edit source]

FMN consists of a riboflavin molecule attached to a phosphate group through a ribose sugar. The riboflavin moiety consists of a tricyclic isoalloxazine ring system, which is responsible for its redox properties. The phosphate group provides a negatively charged moiety, allowing FMN to interact with other molecules in biological systems.

Function[edit | edit source]

As a cofactor, FMN participates in a wide range of enzymatic reactions, particularly those involving oxidation-reduction (redox) reactions. It acts as an electron carrier, shuttling electrons between different enzymes and facilitating the transfer of energy in metabolic pathways.

One of the well-known enzymes that utilize FMN is flavin adenine dinucleotide (FAD) synthase. This enzyme catalyzes the conversion of FMN to FAD, another important cofactor involved in redox reactions.

Role in Metabolism[edit | edit source]

FMN is involved in various metabolic pathways, including the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. In the citric acid cycle, FMN participates in the oxidation of succinate to fumarate by succinate dehydrogenase, an enzyme located in the inner mitochondrial membrane.

In the electron transport chain, FMN acts as an electron carrier between different protein complexes, facilitating the transfer of electrons and the generation of ATP, the energy currency of the cell.

Clinical Significance[edit | edit source]

Deficiencies in FMN can lead to various health conditions, including riboflavin deficiency (also known as ariboflavinosis). Symptoms of riboflavin deficiency may include fatigue, sore throat, and skin disorders.

Furthermore, FMN has been implicated in certain genetic disorders, such as multiple acyl-CoA dehydrogenase deficiency (MADD). MADD is characterized by the impaired function of enzymes that require FMN as a cofactor, leading to metabolic abnormalities and potentially life-threatening complications.

References[edit | edit source]

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Contributors: Prab R. Tumpati, MD