Wikipedia:WikiProject Chemicals/Chembox validation/VerifiedDataSandbox and Flavin mononucleotide: Difference between pages

| 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(2''H'')-yl)-<small>D</small>-ribitol 5-(dihydrogen phosphate)

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

| OtherNames = {{Unbulleted list|FMN}}

|Section1={{Chembox Identifiers

| IUPHAR_ligand = 5185

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

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

| CASNo2 = 130-40-5

| CASNo2_Comment = (sodium salt)

| ChEMBL = 1201794

| PubChem = 643976

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

| 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 [[oxidoreductase]]s, including [[NADH dehydrogenase]], as well as a [[Cofactor (biochemistry)|cofactor]] in biological blue-light photo receptors.<ref>{{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 }}</ref> During the catalytic cycle, a reversible interconversion of the oxidized (FMN), semiquinone (FMNH^•), and reduced (FMNH₂) forms occurs in the various [[Oxidoreductase|oxidoreductases]]. FMN is a stronger oxidizing agent than [[Nicotinamide adenine dinucleotide|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 [[cell (biology)|cell]]s and [[biological tissue|tissues]]. It requires more energy to produce, but is more [[soluble]] than riboflavin. In cells, FMN occurs freely circulating but also in several [[covalent|covalently bound]] forms.<ref name=Mewies>{{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 }}</ref> 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.<ref>{{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 }}</ref><ref>{{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 }}</ref>

==Food additive==

Flavin mononucleotide is also used as an orange-red food colour additive, designated in Europe as [[E number]] E101a.<ref>"[http://www.food.gov.uk/safereating/chemsafe/additivesbranch/enumberlist Current EU approved additives and their E Numbers]", Food Standards Agency website, retrieved 15 Dec 2011</ref>

E106, a very closely related food dye, is riboflavin-5′-phosphate sodium salt, which consists mainly of the [[monosodium]] [[salt (chemistry)|salt]] of the 5′-monophosphate [[ester]] of riboflavin. It is rapidly turned to free riboflavin after [[ingestion]]. It is found in many foods for babies and young children as well as [[jam]]s, [[milk]] products, and sweets and [[sugar]] products.<ref>{{cite journal |doi=10.2903/j.efsa.2017.4919 |title=Dietary Reference Values for riboflavin |year=2017 |last1=Turck |first1=Dominique |last2=Bresson |first2=Jean‐Louis |last3=Burlingame |first3=Barbara |last4=Dean |first4=Tara |last5=Fairweather‐Tait |first5=Susan |last6=Heinonen |first6=Marina |last7=Hirsch‐Ernst |first7=Karen Ildico |last8=Mangelsdorf |first8=Inge |last9=McArdle |first9=Harry J. |last10=Naska |first10=Androniki |last11=Nowicka |first11=Grażyna |last12=Pentieva |first12=Kristina |last13=Sanz |first13=Yolanda |last14=Siani |first14=Alfonso |last15=Sjödin |first15=Anders |last16=Stern |first16=Martin |last17=Tomé |first17=Daniel |last18=Van Loveren |first18=Henk |last19=Vinceti |first19=Marco |last20=Willatts |first20=Peter |last21=Lamberg‐Allardt |first21=Christel |last22=Przyrembel |first22=Hildegard |last23=Tetens |first23=Inge |last24=Dumas |first24=Céline |last25=Fabiani |first25=Lucia |last26=Forss |first26=Annette Cecilia |last27=Ioannidou |first27=Sofia |last28=Neuhäuser‐Berthold |first28=Monika |last29=Neuhäuser-Berthold |display-authors=3 |first29=M. |journal=EFSA Journal |volume=15 |issue=8 |pages=e04919 |pmid=32625611 |pmc=7010026 }}</ref>

==See also==

* [[Flavin adenine dinucleotide]]

==References==

{{Reflist}}

==External links==

*[http://www.ebi.ac.uk/msd-srv/chempdb/cgi-bin/cgi.pl?FUNCTION=getByCode&CODE=FMN FMN] in the [http://www.ebi.ac.uk/msd/ EBI Macromolecular Structure Database]

{{Enzyme cofactors}}

[[Category:Flavins]]

[[Category:Food colorings]]

[[Category:Organophosphates]]

[[Category:Oxidoreductases]]

[[Category:Cofactors]]