Record Information
Version 1.0
Update Date 1/22/2018 11:54:53 AM
Metabolite IDPAMDB000293
Identification
Name: FADH2
Description:FADH2 is a reduced form of Flavin adenine dinucleotide (FAD). FAD is a redox cofactor involved in several important reactions in metabolism. It can exist in two different redox states, which it converts between by accepting or donating electrons. The molecule consists of a riboflavin moiety (vitamin B2) bound to the phosphate group of an ADP molecule. The flavin group is bound to ribitol, a sugar alcohol, by a carbon-nitrogen bond, not a glycosidic bond. Thus, riboflavin is not technically a nucleotide; the name flavin adenine dinucleotide is a misnomer. FAD can be reduced to FADH2, whereby it accepts two hydrogen atoms.
Structure
Thumb
Synonyms:
  • 1,5-Dihydro-FAD
  • 1,5-Dihydro-P-5-ester with adenosine
  • 1,5-dihydro-Riboflavin 5'-(trihydrogen diphosphate) P'->5'-ester with adenosine
  • 1,5-dihydro-Riboflavin 5'-(trihydrogen diphosphoric acid) p'->5'-ester with adenosine
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (8CI)
  • Adenosine 5'-(trihydrogen pyrophosphate), 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-(trihydrogen pyrophosphoric acid), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-(trihydrogen pyrophosphoric acid), 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (8ci)
  • Adenosine 5'-(trihydrogen pyrophosphoric acid), 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine 5'-{3-[D-ribo-5-(7,8-dimethyl-2,4-dioxo-1,2,3,4,5,10-tetrahydrobenzo[g]pteridin-10-yl)-2,3,4-trihydroxypentyl] dihydrogen diphosphate}
  • Adenosine 5'-{3-[D-ribo-5-(7,8-dimethyl-2,4-dioxo-1,2,3,4,5,10-tetrahydrobenzo[g]pteridin-10-yl)-2,3,4-trihydroxypentyl] dihydrogen diphosphoric acid}
  • Adenosine 5-(trihydrogen pyrophosphate)
  • Adenosine 5-(trihydrogen pyrophosphoric acid)
  • Adenosine pyrophosphate 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphate 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (7CI)
  • Adenosine pyrophosphate, 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphate, 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphoric acid 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphoric acid 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine (7ci)
  • Adenosine pyrophosphoric acid, 5'-5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Adenosine pyrophosphoric acid, 5'->5'-ester with 5,10-dihydro-7,8-dimethyl-10-(D-ribo-2,3,4,5-tetrahydroxypentyl)alloxazine
  • Benzo[gr]pteridine riboflavin 5'-(trihydrogen diphosphate) deriv
  • benzo[GR]Pteridine riboflavin 5'-(trihydrogen diphosphoric acid) deriv
  • Benzo[g]pteridine riboflavin 5'-(trihydrogen diphosphate) deriv
  • Benzo[g]pteridine riboflavin 5'-(trihydrogen diphosphate) deriv.
  • benzo[g]Pteridine riboflavin 5'-(trihydrogen diphosphoric acid) deriv
  • benzo[g]Pteridine riboflavin 5'-(trihydrogen diphosphoric acid) deriv.
  • Dihydro-FAD
  • Dihydroflavine-adenine dinucleotide
  • FAD
  • FADH
  • FADH2
  • FDA
  • Flavin adenine dinucleotide (reduced)
  • Flavin adenine dinucleotide reduced
  • Reduced flavine adenine dinucleotide
  • Riboflavin 5'-(trihydrogen diphosphate), 1,5-dihydro-, P'-5'-ester with adenosine
  • Riboflavin 5'-(trihydrogen diphosphate), 1,5-dihydro-, P'-5'-ester with adenosine (9CI)
  • Riboflavin 5'-(trihydrogen diphosphoric acid), 1,5-dihydro-, p'-5'-ester with adenosine
  • Riboflavin 5'-(trihydrogen diphosphoric acid), 1,5-dihydro-, p'-5'-ester with adenosine (9ci)
Chemical Formula: C27H35N9O15P2
Average Molecular Weight: 787.5656
Monoisotopic Molecular Weight: 787.172784519
InChI Key: YPZRHBJKEMOYQH-UYBVJOGSSA-N
InChI:InChI=1S/C27H35N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,32,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H2,33,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
CAS number: 1910-41-4
IUPAC Name:[({[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-1H,2H,3H,4H,5H,10H-benzo[g]pteridin-10-yl}-2,3,4-trihydroxypentyl]oxy})phosphinic acid
Traditional IUPAC Name: fadh(.)
SMILES:CC1=CC2=C(C=C1C)N(C[C@H](O)[C@H](O)[C@H](O)COP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=NC3=C1N=CN=C3N)C1=C(N2)C(=O)NC(=O)N1
Chemical Taxonomy
Taxonomy DescriptionThis compound belongs to the class of organic compounds known as flavin nucleotides. These are nucleotides containing a flavin moiety. Flavin is a compound that contains the tricyclic isoalloxazine ring system, which bears 2 oxo groups at the 2- and 4-positions.
Kingdom Organic compounds
Super ClassNucleosides, nucleotides, and analogues
Class Flavin nucleotides
Sub ClassNot Available
Direct Parent Flavin nucleotides
Alternative Parents
Substituents
  • Flavin nucleotide
  • Purine ribonucleoside diphosphate
  • Flavin
  • Alkyldiarylamine
  • N-glycosyl compound
  • Glycosyl compound
  • Pteridine
  • Organic pyrophosphate
  • Monosaccharide phosphate
  • 6-aminopurine
  • Purine
  • Imidazopyrimidine
  • Monoalkyl phosphate
  • Pyrimidone
  • Aminopyrimidine
  • Imidolactam
  • Benzenoid
  • Alkyl phosphate
  • Pyrimidine
  • Primary aromatic amine
  • Phosphoric acid ester
  • Organic phosphoric acid derivative
  • Organic phosphate
  • N-substituted imidazole
  • Monosaccharide
  • Saccharide
  • Heteroaromatic compound
  • Vinylogous amide
  • Oxolane
  • Imidazole
  • Azole
  • Urea
  • Tertiary amine
  • Secondary alcohol
  • Polyol
  • Lactam
  • 1,2-diol
  • Oxacycle
  • Azacycle
  • Organoheterocyclic compound
  • Secondary amine
  • Hydrocarbon derivative
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Amine
  • Alcohol
  • Aromatic heteropolycyclic compound
Molecular Framework Aromatic heteropolycyclic compounds
External Descriptors
Physical Properties
State: Not Available
Charge:-2
Melting point: Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility2.65 mg/mLALOGPS
logP-0.93ALOGPS
logP-5.4ChemAxon
logS-2.5ALOGPS
pKa (Strongest Acidic)1.86ChemAxon
pKa (Strongest Basic)5ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count18ChemAxon
Hydrogen Donor Count11ChemAxon
Polar Surface Area355.76 Å2ChemAxon
Rotatable Bond Count13ChemAxon
Refractivity188.8 m3·mol-1ChemAxon
Polarizability72.42 Å3ChemAxon
Number of Rings6ChemAxon
Bioavailability0ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations: Cytoplasm
Reactions:
FADH2 + 2 Hydrogen ion + SufBCD with two bound [2Fe-2S] clusters > FAD + SufBCD with bound [4Fe-4S] cluster
FAD + Hydrogen ion + NADPH > FADH2 + NADP
Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD scaffold complex + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with bound [2Fe-2S] cluster +2 SufSE sulfur acceptor complex
Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD with bound [2Fe-2S] cluster + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with two bound [2Fe-2S] clusters +2 SufSE sulfur acceptor complex
FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU scaffold protein > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with bound [2Fe-2S] cluster
FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU with bound [2Fe-2S] cluster > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with two bound [2Fe-2S] clusters
Butyryl-CoA + FAD <> Crotonoyl-CoA + FADH2
FAD + Octanoyl-CoA <> FADH2 + (2E)-Octenoyl-CoA
FAD + Palmityl-CoA <> FADH2 + (2E)-Hexadecenoyl-CoA
FAD + Tetradecanoyl-CoA <> FADH2 + (2E)-Tetradecenoyl-CoA
FAD + Hexanoyl-CoA <> FADH2 + trans-2-Hexenoyl-CoA
FAD + Stearoyl-CoA <> FADH2 + Trans-Octadec-2-enoyl-CoA
Lauroyl-CoA + FAD <> (2E)-Dodecenoyl-CoA + FADH2
Decanoyl-CoA (N-C10:0CoA) + FAD <> (2E)-Decenoyl-CoA + FADH2
FAD + L-Proline > L-D-1-Pyrroline-5-carboxylic acid + FADH2 + Hydrogen ion
D-Alanine + FAD + Water > FADH2 + Ammonium + Pyruvic acid
FADH2 + 2 Hydrogen ion + IscU with two bound [2Fe-2S] clusters > FAD + IscU with bound [4Fe-4S] cluster
FADH2 + 2 Fe3+ > FAD +2 Iron +2 Hydrogen ion
FAD + Hydrogen ion + NADH > FADH2 + NAD
FADH2 + 2 Ferroxamine > FAD +2 Iron +2 ferroxamine minus Fe(3) +2 Hydrogen ion
Succinic acid + FAD <> FADH2 + Fumaric acid
Glycerol 3-phosphate + FAD <> Dihydroxyacetone phosphate + FADH2
Butanoyl-CoA + FAD <> FADH2 + Crotonoyl-CoA
L-Malic acid + FAD <> FADH2 + Oxalacetic acid

Pathways:
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-000i-0001200900-b0740b3d33d50996ccdeView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-000m-0105900000-3abff26d5bb35f8527b8View in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-000i-0931700000-73f360589a13230eea7aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, PositiveNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, NegativeNot Available
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, NegativeNot Available
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Jorns MS: DNA photorepair: chromophore composition and function in two classes of DNA photolyases. Biofactors. 1990 Oct;2(4):207-11. Pubmed: 2282137
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Ramsey AJ, Alderfer JL, Jorns MS: Energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Aug 11;31(31):7134-42. Pubmed: 1643047
  • Ramsey AJ, Jorns MS: Effect of 5-deazaflavin on energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Sep 15;31(36):8437-41. Pubmed: 1390627
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Zeller HD, Hille R, Jorns MS: Bacterial sarcosine oxidase: identification of novel substrates and a biradical reaction intermediate. Biochemistry. 1989 Jun 13;28(12):5145-54. Pubmed: 2475174
Synthesis Reference: Kavakli I Halil; Sancar Aziz Analysis of the role of intraprotein electron transfer in photoreactivation by DNA photolyase in vivo. Biochemistry (2004), 43(48), 15103-10.
Material Safety Data Sheet (MSDS) Not Available
External Links:
ResourceLink
CHEBI ID17877
HMDB IDHMDB01197
Pubchem Compound ID446013
Kegg IDC01352
ChemSpider ID393487
WikipediaFADH
BioCyc IDFADH2
EcoCyc IDFADH2
Ligand ExpoFDA

Enzymes

General function:
Involved in electron carrier activity
Specific function:
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
Gene Name:
sdhB
Locus Tag:
PA1584
Molecular weight:
26.2 kDa
Reactions
Succinate + acceptor = fumarate + reduced acceptor.
General function:
Involved in oxidoreductase activity
Specific function:
Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon
Gene Name:
putA
Locus Tag:
PA0782
Molecular weight:
115.6 kDa
Reactions
L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
(S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2 H(2)O = L-glutamate + NAD(P)H.
General function:
Involved in metabolic process
Specific function:
Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for NAD, biotin and Fe-S cluster synthesis. Transfers sulfur on 'Cys-456' of thiI in a transpersulfidation reaction. Transfers sulfur on 'Cys-19' of tusA in a transpersulfidation reaction. Functions also as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate
Gene Name:
iscS
Locus Tag:
PA3814
Molecular weight:
44.7 kDa
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
General function:
Involved in D-amino-acid dehydrogenase activity
Specific function:
Oxidative deamination of D-amino acids
Gene Name:
dadA
Locus Tag:
PA5304
Molecular weight:
47.1 kDa
Reactions
A D-amino acid + H(2)O + acceptor = a 2-oxo acid + NH(3) + reduced acceptor.
General function:
Involved in electron carrier activity
Specific function:
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth
Gene Name:
sdhA
Locus Tag:
PA1583
Molecular weight:
63.5 kDa
Reactions
Succinate + acceptor = fumarate + reduced acceptor.
General function:
Involved in succinate dehydrogenase activity
Specific function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH)
Gene Name:
sdhD
Locus Tag:
PA1582
Molecular weight:
13.7 kDa
General function:
Involved in oxidoreductase activity
Specific function:
Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor
Gene Name:
glpD
Locus Tag:
PA3584
Molecular weight:
57.1 kDa
Reactions
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
General function:
Involved in sulfite reductase (NADPH) activity
Specific function:
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L- cysteine from sulfate
Gene Name:
cysI
Locus Tag:
PA1838
Molecular weight:
62.1 kDa
Reactions
H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.
General function:
Involved in malate dehydrogenase (quinone) activity
Specific function:
(S)-malate + a quinone = oxaloacetate + reduced quinone
Gene Name:
mqo
Locus Tag:
PA3452
Molecular weight:
57.2 kDa
Reactions
(S)-malate + a quinone = oxaloacetate + reduced quinone.
General function:
Involved in succinate dehydrogenase activity
Specific function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH)
Gene Name:
sdhC
Locus Tag:
PA1581
Molecular weight:
13.7 kDa
General function:
Involved in acyl-CoA dehydrogenase activity
Specific function:
Catalyzes the dehydrogenation of acyl-CoA
Gene Name:
fadE
Locus Tag:
PA2815
Molecular weight:
88.8 kDa
Reactions
An acyl-CoA + FAD = a dehydrogenated acyl-CoA + FADH(2).
General function:
Involved in iron ion binding
Specific function:
May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins (Potential)
Gene Name:
nifU
Locus Tag:
PA3813
Molecular weight:
13.8 kDa

Transporters