Record Information
Version2.0
Creation Date2012-05-31 13:58:01 -0600
Update Date2015-06-03 15:54:20 -0600
Secondary Accession Numbers
  • ECMDB03178
Identification
Name:Heme
DescriptionHeme 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.
Structure
Thumb
Synonyms:
  • (protoporphyrinato)iron
  • Ferroheme
  • Ferroheme b
  • Ferroprotoheme
  • Ferroprotoporphyrin
  • Ferroprotoporphyrin IX
  • Ferrous protoheme
  • Ferrous protoheme IX
  • Haem
  • Hem
  • Heme
  • Heme b
  • Heme b
  • Iron protoporphyrin
  • Iron protoporphyrin IX
  • Iron(II) protoporphyrin IX
  • Protoferroheme
  • Protohaem
  • Protoheme
  • Protoheme IX
  • Reduced hematin
Chemical Formula:C34H32FeN4O4
Weight:Average: 616.487
Monoisotopic: 616.177297665
InChI Key:YHLKGEDAGPGZPN-RGGAHWMASA-L
InChI:InChI=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-;
CAS number:14875-96-8
IUPAC Name:4,20-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-diuide
Traditional IUPAC Name:4,20-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-diuide
SMILES:CC1=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)=O
Chemical Taxonomy
ClassificationNot classified
Physical Properties
State:Solid
Charge:-2
Melting point:Not Available
Experimental Properties:
PropertyValueSource
Predicted Properties
PropertyValueSource
Water Solubility0.0024 g/LALOGPS
logP-1ALOGPS
logP2.19ChemAxon
logS-5.5ALOGPS
pKa (Strongest Acidic)3.35ChemAxon
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area92.22 ŲChemAxon
Rotatable Bond Count8ChemAxon
Refractivity169.77 m³·mol⁻¹ChemAxon
Polarizability69.44 ųChemAxon
Number of Rings8ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations:Cytoplasm
Reactions:
SMPDB Pathways:Not Available
KEGG Pathways:
EcoCyc Pathways:
Concentrations
Not Available
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (1 TMS) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TMS_2_1) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TBDMS_1_1) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TBDMS_1_2) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS (TBDMS_2_1) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted GC-MSPredicted GC-MS Spectrum - GC-MS ("Heme,1TMS,#1" TMS) - 70eV, PositiveNot AvailableView in JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-066r-0000095000-501c4a776d38d61ab89aView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0gi4-0000092000-64c21d0a0f8daa069fb9View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-03gs-4000590000-15136ce22e51bdc57377View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-014i-0000049000-69ee302652cebc40f13bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00r2-1000091000-d178bb83079a203a48dcView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0a4i-1000090000-f6e437751fbc08f12d1fView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-014j-0000059000-0ab427d87ba10992d498View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-014i-0000098000-650f7d2f023028ff2319View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-06fr-0000090000-2dff1da74eb12a246237View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-014j-0000079000-990502ea40621d9cad46View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-05ns-0000091000-3547d5c809ccf8987200View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0cdr-0000092000-e55d1ab39076367d5b9eView in MoNA
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR1H NMR SpectrumNot AvailableView in JSpectraViewer
1D NMR13C NMR SpectrumNot AvailableView in JSpectraViewer
References
References:
  • Allhorn 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. Pubmed: 12925227
  • 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
  • Kuhnel A, Gross U, Doss MO: Hereditary coproporphyria in Germany: clinical-biochemical studies in 53 patients. Clin Biochem. 2000 Aug;33(6):465-73. Pubmed: 11074238
  • Ono 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. Pubmed: 15955097
  • Park 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. Pubmed: 14644357
  • Taylor 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. Pubmed: 8944032
  • 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
  • Walczyk T, von Blanckenburg F: Natural iron isotope variations in human blood. Science. 2002 Mar 15;295(5562):2065-6. Pubmed: 11896276
  • Winder, 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. Pubmed: 18331064
  • Zhang JP, Normark S: Induction of gene expression in Escherichia coli after pilus-mediated adherence. Science. 1996 Aug 30;273(5279):1234-6. Pubmed: 8703059
Synthesis Reference:Not Available
Material Safety Data Sheet (MSDS)Not Available
External Links:
ResourceLink
CHEBI ID17627
HMDB IDHMDB03178
Pubchem Compound ID26945
Kegg IDC00032
ChemSpider IDNot Available
WikipediaHeme
BioCyc IDPROTOHEME
EcoCyc IDPROTOHEME

Enzymes

General function:
Involved in ferrochelatase activity
Specific function:
Catalyzes the ferrous insertion into protoporphyrin IX
Gene Name:
hemH
Uniprot ID:
P23871
Molecular weight:
35884
Reactions
Protoheme + 2 H(+) = protoporphyrin + Fe(2+).
General function:
Involved in nucleotide binding
Specific function:
Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system
Gene Name:
ccmA
Uniprot ID:
P33931
Molecular weight:
23053
Reactions
ATP + H(2)O + heme(In) = ADP + phosphate + heme(Out).
General function:
Involved in protein complex assembly
Specific function:
Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes
Gene Name:
ccmC
Uniprot ID:
P0ABM1
Molecular weight:
27885
General function:
Involved in heme transporter activity
Specific function:
Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes
Gene Name:
ccmB
Uniprot ID:
P0ABL8
Molecular weight:
23618
General function:
Involved in transport
Specific function:
Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes (Potential)
Gene Name:
ccmD
Uniprot ID:
P0ABM5
Molecular weight:
7745
General function:
Involved in protoheme IX farnesyltransferase activity
Specific function:
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group
Gene Name:
cyoE
Uniprot ID:
P0AEA5
Molecular weight:
32248
General function:
Involved in protein-heme linkage
Specific function:
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH
Gene Name:
ccmE
Uniprot ID:
P69490
Molecular weight:
17698