Coenzyme f420

Coenzyme F420 (molecular formula: C29H32N5O18P4), also known as cofactor F420, is an enzyme belonging to the family of oxidoreductases. The enzyme is found in the cytoplasm of methanogenic archaea, some bacteria and unicellular eukaryotes. It has 3 cofactors: iron, nickel and deazaflavin (Deppenmeier U 2002).

Biochemically it is an electron transporter, and chemically it is a deazaflavin, similar to riboflavin. F420 is involved in processes such as methanogenesis, sulfite reduction and oxygen detoxification. F420 is a cofactor in the synthesis of antibiotics in streptomycetes. For example, coenzyme F420 is responsible for the reduction of pretomanide (in mycobacteria). In order for Pretomanid to develop its effect against mycobacteria, the substance must be activated by a reduction of an aromatic nitro group. This is done via the coenzyme F420 of the tuberculosis pathogen Mycobacterium tuberculosis (Mashalidis EH et al. 2015).

For the regeneration of oxidized F420 an enzyme is needed, which is called F420-reducing hydrogenase. This enzyme is either frequently membrane-bound or occasionally localised in the cytoplasm.

F420 owes its name to its strong light absorption at a wavelength of 420 nm.

1. Deppenmeier U (2002): The Unique Biochemistry of Methanogenesis. In: Prog Nucleic Acid Res Mol Biol. 71: 223-83
2. Deppenmeier U (2002): Redox-driven proton translocation in methanogenic archaea. In: Cell Mol Life Sci 59: 1513-1533
3. Greening C et al (2016) Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions. Microbiology and molecular biology reviews. MMBR 80: 451-493.
4. Mashalidis EH et al (2015) Molecular insights into the binding of coenzyme F420 to the conserved protein Rv1155 from Mycobacterium tuberculosis. Protein science 24: 729-740.