:Flavin mononucleotide

{{chembox

| Verifiedfields = changed

| Watchedfields = changed

| verifiedrevid = 461100522

| ImageFile = Flavin mononucleotide v2.svg

| ImageSize = 180

| ImageAlt = Skeletal formula of flavin mononucleotide

| ImageFile1 = Flavin mononucleotide 3D ball.png

| ImageSize1 = 180

| ImageAlt1 = Ball-and-stick model of the flavin mononucleotide molecule

| IUPACName = 1-Deoxy-1-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-D-ribitol 5-(dihydrogen phosphate)

| SystematicName = (2R,3S,4S)-5-(7,8-Dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-2,3,4-trihydroxypentyl dihydrogen phosphate

| OtherNames = {{Unbulleted list|FMN}}

|Section1={{Chembox Identifiers

| IUPHAR_ligand = 5185

| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}

| ChemSpiderID = 559060

| UNII_Ref = {{fdacite|correct|FDA}}

| UNII = 7N464URE7E

| StdInChI_Ref = {{stdinchicite|correct|chemspider}}

| StdInChI = 1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1

| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}

| StdInChIKey = FVTCRASFADXXNN-SCRDCRAPSA-N

| CASNo_Ref = {{cascite|correct|CAS}}

| CASNo = 146-17-8

| CASNo2_Ref = {{cascite|correct|CAS}}

| CASNo2 = 130-40-5

| CASNo2_Comment = (sodium salt)

| ChEMBL_Ref = {{ebicite|changed|EBI}}

| ChEMBL = 1201794

| PubChem = 643976

| ChEBI_Ref = {{ebicite|correct|EBI}}

| ChEBI = 17621

| SMILES = Cc1cc2c(cc1C)n(c-3nc(=O)[nH]c(=O)c3n2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O

| MeSHName = Flavin+mononucleotide

}}

|Section2={{Chembox Properties

| Formula = C₁₇H₂₁N₄O₉P

| MolarMass = 456.344 g/mol

| Appearance =

| Density =

| MeltingPt = 195 °C

| BoilingPt =

}}

|Section3={{Chembox Hazards

| MainHazards =

| FlashPt =

| AutoignitionPt =

}}

}}

{{More citations needed|date=December 2009}}

Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B₂) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors.{{cite journal|title=Studies on the Binding and Function of Flavin Phosphates with Flavin Mononucleotide-dependent Enzymes|first1=John C. M. |last1=Tsibris|first2= Donald B. |last2=McCormick |first3= Lemuel D.|last3= Wright|journal=Journal of Biological Chemistry|year=1966 |volume=241 |issue=5 |pages=1138–43 |doi=10.1016/S0021-9258(18)96813-4 |pmid=4379862 |doi-access=free }} During the catalytic cycle, various oxidoreductases induce reversible interconversions between the oxidized (FMN), semiquinone (FMNH^•), and reduced (FMNH₂) forms of the isoalloxazine core. FMN is a stronger oxidizing agent than NAD and is particularly useful because it can take part in both one- and two-electron transfers. In its role as blue-light photo receptor, (oxidized) FMN stands out from the 'conventional' photo receptors as the signaling state and not an E/Z isomerization.

It is the principal form in which riboflavin is found in cells and tissues. It requires more energy to produce, but is more soluble than riboflavin. In cells, FMN occurs freely circulating but also in several covalently bound forms.{{cite journal |doi=10.1002/pro.5560070102 |doi-access=free |title=Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs |year=1998 |vauthors=Mewies M, McIntire WS, Scrutton NS |journal=Protein Science |volume=7 |issue=1 |pages=7–20 |pmid=9514256 |pmc=2143808 }} Covalently or non-covalently bound FMN is a cofactor of many enzymes playing an important pathophysiological role in cellular metabolism. For example dissociation of flavin mononucleotide from mitochondrial complex I has been shown to occur during ischemia/reperfusion brain injury during stroke.{{cite journal |last1=Kahl |first1=A |last2=Stepanova |first2=A |last3=Konrad |first3=C |last4=Anderson |first4=C |last5=Manfredi |first5=G |last6=Zhou |first6=P |last7=Iadecola |first7=C |last8=Galkin |first8=A |title=Critical Role of Flavin and Glutathione in Complex I-Mediated Bioenergetic Failure in Brain Ischemia/Reperfusion Injury. |journal=Stroke |date=2018 |volume=49 |issue=5 |pages=1223–1231 |doi=10.1161/STROKEAHA.117.019687 |pmid=29643256|pmc=5916474 }}{{cite journal |last1=Galkin |first1=A |title=Brain Ischemia/Reperfusion Injury and Mitochondrial Complex I Damage. |journal=Biochemistry. Biokhimiia |date=2019 |volume=84 |issue=11 |pages=1411–1423 |doi=10.1134/S0006297919110154 |pmid=31760927|s2cid=207990089 }}