2.02012-05-31 13:58:01 -06002015-06-03 15:54:20 -0600ECMDB03178M2MDB000481HemeHeme B or haem B (also known as protoheme IX) is the most abundant heme in nature. E. coli is known to produce 4 different hemes: protoheme IX (heme B), heme C, heme D, and siroheme. A heme or haem is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. Not all porphyrins contain iron, but a substantial fraction of porphyrin-containing metalloproteins have heme as their prosthetic subunit; these are known as hemoproteins. Generally, heme B is attached to the surrounding protein matrix (known as the apoprotein) through a single coordination bond between the heme iron and an amino-acid side-chain. When oxygen is bound the iron becomes hexacoordinated. Since the iron in heme B containing proteins is bound to the four nitrogens of the porphyrin (forming a plane) and a single electron donating atom of the protein, the iron is often in a pentacoordinate state.(protoporphyrinato)ironFerrohemeFerroheme bFerroprotohemeFerroprotoporphyrinFerroprotoporphyrin IXFerrous protohemeFerrous protoheme IXHaemHemHemeHeme <i>b</i>Heme bIron protoporphyrinIron protoporphyrin IXIron(II) protoporphyrin IXProtoferrohemeProtohaemProtohemeProtoheme IXReduced hematinC34H32FeN4O4616.487616.1772976654,20-bis(2-carboxyethyl)-10,15-diethenyl-5,9,14,19-tetramethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)-1,1-diuide4,20-bis(2-carboxyethyl)-10,15-diethenyl-5,9,14,19-tetramethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)-1,1-diuide14875-96-8CC1=C(CCC(O)=O)C2=CC3=[N+]4C(=CC5=C(C=C)C(C)=C6C=C7C(C=C)=C(C)C8=[N+]7[Fe@]4(N2C1=C8)N56)C(C)=C3CCC(O)=OInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+4/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;YHLKGEDAGPGZPN-RGGAHWMASA-LSolidCytosolExtra-organismMembranePeriplasmlogp-1.01logs-5.48solubility2.42e-03 g/llogp2.19pka_strongest_acidic3.35iupac4,20-bis(2-carboxyethyl)-10,15-diethenyl-5,9,14,19-tetramethyl-2lambda5,22,23lambda5,25-tetraaza-1-ferraoctacyclo[11.9.1.1^{1,8}.1^{3,21}.0^{2,6}.0^{16,23}.0^{18,22}.0^{11,25}]pentacosa-2,4,6,8,10,12,14,16(23),17,19,21(24)-undecaene-2,23-bis(ylium)-1,1-diuideaverage_mass616.487mono_mass616.177297665smilesCC1=C(CCC(O)=O)C2=CC3=[N+]4C(=CC5=C(C=C)C(C)=C6C=C7C(C=C)=C(C)C8=[N+]7[Fe@]4(N2C1=C8)N56)C(C)=C3CCC(O)=OformulaC34H32FeN4O4inchiInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+4/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;inchikeyYHLKGEDAGPGZPN-RGGAHWMASA-Lpolar_surface_area92.22refractivity169.77polarizability69.44rotatable_bond_count8acceptor_count4donor_count2physiological_charge-2formal_charge0Porphyrin and chlorophyll metabolismec00860ABC transportersec02010Metabolic pathwayseco01100heme biosynthesis from uroporphyrinogen-III IHEME-BIOSYNTHESIS-IIsuperpathway of heme biosynthesis from uroporphyrinogen-IIIPWY0-1415heme biosynthesis from uroporphyrinogen-III IIHEMESYN2-PWYSpecdb::CMs103503Specdb::CMs103504Specdb::CMs540170Specdb::CMs540171Specdb::CMs540172Specdb::CMs540173Specdb::CMs792693Specdb::NmrOneD135300Specdb::NmrOneD135301Specdb::NmrOneD135302Specdb::NmrOneD135303Specdb::NmrOneD135304Specdb::NmrOneD135305Specdb::NmrOneD135306Specdb::NmrOneD135307Specdb::NmrOneD135308Specdb::NmrOneD135309Specdb::NmrOneD135310Specdb::NmrOneD135311Specdb::NmrOneD135312Specdb::NmrOneD135313Specdb::NmrOneD135314Specdb::NmrOneD135315Specdb::NmrOneD135316Specdb::NmrOneD135317Specdb::NmrOneD135318Specdb::NmrOneD135319Specdb::MsMs1223065Specdb::MsMs1223066Specdb::MsMs1223067Specdb::MsMs1338706Specdb::MsMs1338707Specdb::MsMs1338708Specdb::MsMs2302812Specdb::MsMs2302813Specdb::MsMs2302814Specdb::MsMs3066725Specdb::MsMs3066726Specdb::MsMs3066727HMDB0317826945C0003217627PROTOHEMEHemeKeseler, 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-D590.21097882Kanehisa, 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-D114.22080510van 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 370:17-25.17765195Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948.18331064Ono F, Sharma BK, Smith CC, Burnett JW, Aurelian L: CD34+ cells in the peripheral blood transport herpes simplex virus DNA fragments to the skin of patients with erythema multiforme (HAEM). J Invest Dermatol. 2005 Jun;124(6):1215-24.15955097Allhorn M, Lundqvist K, Schmidtchen A, Akerstrom B: Heme-scavenging role of alpha1-microglobulin in chronic ulcers. J Invest Dermatol. 2003 Sep;121(3):640-6.12925227Walczyk T, von Blanckenburg F: Natural iron isotope variations in human blood. Science. 2002 Mar 15;295(5562):2065-6.11896276Kuhnel A, Gross U, Doss MO: Hereditary coproporphyria in Germany: clinical-biochemical studies in 53 patients. Clin Biochem. 2000 Aug;33(6):465-73.11074238Zhang JP, Normark S: Induction of gene expression in Escherichia coli after pilus-mediated adherence. Science. 1996 Aug 30;273(5279):1234-6.8703059Taylor TD, Litt M, Kramer P, Pandolfo M, Angelini L, Nardocci N, Davis S, Pineda M, Hattori H, Flett PJ, Cilio MR, Bertini E, Hayflick SJ: Homozygosity mapping of Hallervorden-Spatz syndrome to chromosome 20p12.3-p13. Nat Genet. 1996 Dec;14(4):479-81.8944032Park KK, Park JH, Jung YJ, Chung WY: Inhibitory effects of chlorophyllin, hemin and tetrakis(4-benzoic acid)porphyrin on oxidative DNA damage and mouse skin inflammation induced by 12-O-tetradecanoylphorbol-13-acetate as a possible anti-tumor promoting mechanism. Mutat Res. 2003 Dec 9;542(1-2):89-97.14644357FerrochelataseP23871HEMH_ECOLIhemHhttp://ecmdb.ca/proteins/P23871.xmlCytochrome c biogenesis ATP-binding export protein CcmAP33931CCMA_ECOLIccmAhttp://ecmdb.ca/proteins/P33931.xmlHeme exporter protein CP0ABM1CCMC_ECOLIccmChttp://ecmdb.ca/proteins/P0ABM1.xmlHeme exporter protein BP0ABL8CCMB_ECOLIccmBhttp://ecmdb.ca/proteins/P0ABL8.xmlHeme exporter protein DP0ABM5CCMD_ECOLIccmDhttp://ecmdb.ca/proteins/P0ABM5.xmlProtoheme IX farnesyltransferaseP0AEA5CYOE_ECOLIcyoEhttp://ecmdb.ca/proteins/P0AEA5.xmlCytochrome c-type biogenesis protein CcmEP69490CCME_ECOLIccmEhttp://ecmdb.ca/proteins/P69490.xmlAdenosine triphosphate + Water + Heme > ADP + Hydrogen ion + Phosphate + HemeTRANS-RXN0-162Adenosine triphosphate + Water + Heme > ADP + Hydrogen ion + Phosphate + HemeTRANS-RXN0-162Farnesyl pyrophosphate + Water + Heme > Heme O + PyrophosphateR07411HEMEOSYN-RXNIron + Protoporphyrin IX >2 Hydrogen ion + HemePROTOHEMEFERROCHELAT-RXNProtoporphyrin IX + Fe2+ <> Heme +2 Hydrogen ion + Fe2+R00310Heme + Water + Farnesyl pyrophosphate <> Heme O + PyrophosphateR07411HEMEOSYN-RXNHeme + Hydrogen peroxide Heme DRXN-8073Hydrogen ion + Heme Protoporphyrin IX + IronRXN0-6258Iron + Protoporphyrin IX > Heme + Hydrogen ionPROTOHEMEFERROCHELAT-RXNHeme + Adenosine triphosphate + Water > Phosphate + ADP + Heme + Hydrogen ionTRANS-RXN0-162Heme + Adenosine triphosphate + Water > Phosphate + ADP + Heme + Hydrogen ionTRANS-RXN0-162Heme + 2 Hydrogen ion > Protoporphyrin IX + IronADP + Phosphate + 4 Hydrogen ion + Heme + Nickel(2+) + Iron chelate + Taurine + Molybdate + Magnesium + Fe3+ + Potassium + Polyamine + vitamin B12 + Sulfate + glycerol-3-phosphate + Phosphonate + D-Maltose <> Adenosine triphosphate +3 Hydrogen ion + WaterR00086RXN0-1061Farnesyl pyrophosphate + Water + Heme > Heme O + PyrophosphateProtoporphyrin IX + Fe2+ <> Heme +2 Hydrogen ionFarnesyl pyrophosphate + Water + Heme > Heme O + Pyrophosphate