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 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
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