2.0 2012-05-31 13:47:23 -0600 2015-09-13 15:15:22 -0600 ECMDB01197 M2MDB000293 FADH2 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. 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) C27H35N9O15P2 787.5656 787.172784519 {[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(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}(hydroxy)phosphoryl)oxy]phosphinic acid fadh(.) 1910-41-4 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 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 YPZRHBJKEMOYQH-UYBVJOGSSA-N Cytosol logp -0.23 ALOGPS logs -2.37 ALOGPS solubility 3.39e+00 g/l ALOGPS logp -4.8 ChemAxon pka_strongest_acidic 1.85 ChemAxon pka_strongest_basic 4.01 ChemAxon iupac {[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}[({[(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}(hydroxy)phosphoryl)oxy]phosphinic acid ChemAxon average_mass 787.5656 ChemAxon mono_mass 787.172784519 ChemAxon 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 ChemAxon formula C27H35N9O15P2 ChemAxon 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 ChemAxon inchikey YPZRHBJKEMOYQH-UYBVJOGSSA-N ChemAxon polar_surface_area 355.76 ChemAxon refractivity 188.8 ChemAxon polarizability 69.69 ChemAxon rotatable_bond_count 13 ChemAxon acceptor_count 18 ChemAxon donor_count 11 ChemAxon physiological_charge -2 ChemAxon formal_charge 0 ChemAxon Riboflavin metabolism ec00740 Specdb::CMs 65421 Specdb::CMs 786399 Specdb::CMs 786400 Specdb::CMs 786401 Specdb::CMs 786402 Specdb::CMs 786403 Specdb::CMs 786404 Specdb::CMs 786405 Specdb::CMs 786406 Specdb::CMs 786407 Specdb::CMs 786408 Specdb::CMs 786409 Specdb::NmrOneD 1659 Specdb::NmrOneD 146810 Specdb::NmrOneD 146811 Specdb::NmrOneD 146812 Specdb::NmrOneD 146813 Specdb::NmrOneD 146814 Specdb::NmrOneD 146815 Specdb::NmrOneD 146816 Specdb::NmrOneD 146817 Specdb::NmrOneD 146818 Specdb::NmrOneD 146819 Specdb::NmrOneD 146820 Specdb::NmrOneD 146821 Specdb::NmrOneD 146822 Specdb::NmrOneD 146823 Specdb::NmrOneD 146824 Specdb::NmrOneD 146825 Specdb::NmrOneD 146826 Specdb::NmrOneD 146827 Specdb::NmrOneD 146828 Specdb::NmrOneD 146829 Specdb::MsMs 1457 Specdb::MsMs 1458 Specdb::MsMs 1459 Specdb::MsMs 179277 Specdb::MsMs 179278 Specdb::MsMs 179279 Specdb::MsMs 181602 Specdb::MsMs 181603 Specdb::MsMs 181604 Specdb::MsMs 2336158 Specdb::MsMs 2336159 Specdb::MsMs 2336160 Specdb::MsMs 2629481 Specdb::MsMs 2629482 Specdb::MsMs 2629483 Specdb::NmrTwoD 1056 Specdb::NmrTwoD 1600 HMDB01197 393487 C01352 17877 FADH2 FDA FADH 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. 21097882 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. 22080510 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. 17765195 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. 17379776 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. 2475174 Ramsey AJ, Alderfer JL, Jorns MS: Energy transduction during catalysis by Escherichia coli DNA photolyase. Biochemistry. 1992 Aug 11;31(31):7134-42. 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. 1390627 Jorns MS: DNA photorepair: chromophore composition and function in two classes of DNA photolyases. Biofactors. 1990 Oct;2(4):207-11. 2282137 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. Fumarate reductase flavoprotein subunit P00363 FRDA_ECOLI frdA http://ecmdb.ca/proteins/P00363.xml Succinate dehydrogenase iron-sulfur subunit P07014 DHSB_ECOLI sdhB http://ecmdb.ca/proteins/P07014.xml Bifunctional protein putA P09546 PUTA_ECOLI putA http://ecmdb.ca/proteins/P09546.xml Cysteine desulfurase P0A6B7 ISCS_ECOLI iscS http://ecmdb.ca/proteins/P0A6B7.xml D-amino acid dehydrogenase small subunit P0A6J5 DADA_ECOLI dadA http://ecmdb.ca/proteins/P0A6J5.xml Fumarate reductase subunit C P0A8Q0 FRDC_ECOLI frdC http://ecmdb.ca/proteins/P0A8Q0.xml Fumarate reductase subunit D P0A8Q3 FRDD_ECOLI frdD http://ecmdb.ca/proteins/P0A8Q3.xml Anaerobic glycerol-3-phosphate dehydrogenase subunit C P0A996 GLPC_ECOLI glpC http://ecmdb.ca/proteins/P0A996.xml Anaerobic glycerol-3-phosphate dehydrogenase subunit A P0A9C0 GLPA_ECOLI glpA http://ecmdb.ca/proteins/P0A9C0.xml Succinate dehydrogenase flavoprotein subunit P0AC41 DHSA_ECOLI sdhA http://ecmdb.ca/proteins/P0AC41.xml Succinate dehydrogenase hydrophobic membrane anchor subunit P0AC44 DHSD_ECOLI sdhD http://ecmdb.ca/proteins/P0AC44.xml Fumarate reductase iron-sulfur subunit P0AC47 FRDB_ECOLI frdB http://ecmdb.ca/proteins/P0AC47.xml NAD(P)H-flavin reductase P0AEN1 FRE_ECOLI fre http://ecmdb.ca/proteins/P0AEN1.xml Anaerobic glycerol-3-phosphate dehydrogenase subunit B P13033 GLPB_ECOLI glpB http://ecmdb.ca/proteins/P13033.xml Aerobic glycerol-3-phosphate dehydrogenase P13035 GLPD_ECOLI glpD http://ecmdb.ca/proteins/P13035.xml Sulfite reductase [NADPH] hemoprotein beta-component P17846 CYSI_ECOLI cysI http://ecmdb.ca/proteins/P17846.xml Malate:quinone oxidoreductase P33940 MQO_ECOLI mqo http://ecmdb.ca/proteins/P33940.xml Sulfite reductase [NADPH] flavoprotein alpha-component P38038 CYSJ_ECOLI cysJ http://ecmdb.ca/proteins/P38038.xml Ferric iron reductase protein fhuF P39405 FHUF_ECOLI fhuF http://ecmdb.ca/proteins/P39405.xml Succinate dehydrogenase cytochrome b556 subunit P69054 DHSC_ECOLI sdhC http://ecmdb.ca/proteins/P69054.xml Cysteine desulfurase_ P77444 SUFS_ECOLI sufS http://ecmdb.ca/proteins/P77444.xml Acyl-coenzyme A dehydrogenase Q47146 FADE_ECOLI fadE http://ecmdb.ca/proteins/Q47146.xml Probable ATP-dependent transporter sufC P77499 SUFC_ECOLI sufC http://ecmdb.ca/proteins/P77499.xml FeS cluster assembly protein sufB P77522 SUFB_ECOLI sufB http://ecmdb.ca/proteins/P77522.xml Protein cyaY P27838 CYAY_ECOLI cyaY http://ecmdb.ca/proteins/P27838.xml NifU-like protein P0ACD4 NIFU_ECOLI nifU http://ecmdb.ca/proteins/P0ACD4.xml Cysteine desulfuration protein sufE P76194 SUFE_ECOLI sufE http://ecmdb.ca/proteins/P76194.xml FeS cluster assembly protein sufD P77689 SUFD_ECOLI sufD http://ecmdb.ca/proteins/P77689.xml Probable ATP-dependent transporter sufC P77499 SUFC_ECOLI sufC http://ecmdb.ca/proteins/P77499.xml 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 R03777 FAD + Palmityl-CoA <> FADH2 + (2E)-Hexadecenoyl-CoA R01279 FAD + Tetradecanoyl-CoA <> FADH2 + (2E)-Tetradecenoyl-CoA R03990 FAD + Hexanoyl-CoA <> FADH2 + trans-2-Hexenoyl-CoA R04751 FAD + Stearoyl-CoA <> FADH2 + Trans-Octadec-2-enoyl-CoA Lauroyl-CoA + FAD <> (2E)-Dodecenoyl-CoA + FADH2 R03857 Decanoyl-CoA (N-C10:0CoA) + FAD <> (2E)-Decenoyl-CoA + FADH2 R04754 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 R00408 Glycerol 3-phosphate + FAD <> Dihydroxyacetone phosphate + FADH2 R00848 Butanoyl-CoA + FAD <> FADH2 + Crotonoyl-CoA R01175 L-Malic acid + FAD <> FADH2 + Oxalacetic acid R01257 Succinic acid + Ubiquinone-10 + FAD <> Fumaric acid + QH2 + FADH2 PW_R002582 Succinic acid + FAD <> FADH2 + Fumaric acid FAD + Octanoyl-CoA <> FADH2 + (2E)-Octenoyl-CoA L-Malic acid + FAD <> FADH2 + Oxalacetic acid Glycerol 3-phosphate + FAD <> Dihydroxyacetone phosphate + FADH2 Succinic acid + FAD <> FADH2 + Fumaric acid Succinic acid + FAD <> FADH2 + Fumaric acid FAD + Octanoyl-CoA <> FADH2 + (2E)-Octenoyl-CoA L-Malic acid + FAD <> FADH2 + Oxalacetic acid 48 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L Gluco Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h 37.7 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 150800 0 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. 17379776