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Record Information
Creation Date2009-07-25 00:10:23 UTC
Update Date2013-02-08 18:40:29 UTC
Secondary Accession NumbersNone
Metabolite Identification
Common NameFerrocytochrome
DescriptionFerricytochrome is a cytochrome containing reduced (ferrous) iron. Cytochrome c is an electron-carrying protein found in mitochondria of all aerobic organisms. It is part of the terminal oxidation chain, which completes the breakdown of foods to COZ and HzO, storing the liberated chemical energy in molecules of ATP. Like myoglobin, it is an iron porphyrin protein, made up of one heme group and one polypeptide chain. The iron atomalternates between the +2 and +3 oxidation state as the molecule interacts in turn with cytochrome reductase and cytochrome oxidase, each a large multimolecular complex (l-3). One of the goals of the present x-ray analysis is to understand how electron. transfer occurs into and out of cytochrome c, which will ultimately require a knowledge of the molecular structure in both the ferric and ferrous states.
  1. 553-12-8 (FREE ACID)
  2. Ferrocytochrome b-561
  3. H2ppIX
  4. HEM
  5. Kammerer'S porphyrin
  6. Kammerer'S prophyrin
  7. Lopac-P-8293
  8. NSC2632 (FREE ACID)
  9. Ooporphyrin
  10. Porphyrinogen ix
  11. PP-ix
  12. Protoporhyrin ix
  13. Protoporphyrin
  14. Protoporphyrin (PP)
  15. Protoporphyrin ix
  16. Protoporphyrin IX (6CI)
  17. Protoporphyrin IX (van)
  18. Protoporphyrin IX disodium
  19. Protoporphyrin-1x
  20. Protoporpyrin ix
Chemical FormulaC33H32FeN4O4
Average Molecular Weight604.477
Monoisotopic Molecular Weight604.177297665
IUPAC NameNot Available
Traditional NameNot Available
CAS Registry Number1818-68-4
InChI Identifier
Chemical Taxonomy
ClassificationNot classified
StatusExpected but not Quantified
  • Endogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locationsNot Available
Physical Properties
Experimental Properties
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
Water Solubility0.15 mg/mLALOGPS
Physiological Charge-2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area121.19 Å2ChemAxon
Rotatable Bond Count7ChemAxon
Refractivity171.54 m3·mol-1ChemAxon
Polarizability68.6 Å3ChemAxon
Number of Rings8ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
SpectraNot Available
Biological Properties
Cellular LocationsNot Available
Biofluid LocationsNot Available
Tissue LocationNot Available
PathwaysNot Available
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
Associated Disorders and Diseases
Disease ReferencesNone
Associated OMIM IDsNone
DrugBank IDNot Available
DrugBank Metabolite IDNot Available
Phenol Explorer Compound IDNot Available
Phenol Explorer Metabolite IDNot Available
FoodDB IDFDB029223
KNApSAcK IDNot Available
Chemspider IDNot Available
KEGG Compound IDC05183
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkNot Available
NuGOwiki LinkHMDB12947
Metagene LinkHMDB12947
METLIN IDNot Available
PubChem CompoundNot Available
PDB IDNot Available
ChEBI ID15910
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Gederaas OA, Berg K, Romslo I: A comparative study of normal and reverse phase high pressure liquid chromatography for analysis of porphyrins accumulated after 5-aminolaevulinic acid treatment of colon adenocarcinoma cells. Cancer Lett. 2000 Mar 31;150(2):205-13. [10704744 ]
  2. Desuzinges-Mandon E, Arnaud O, Martinez L, Huche F, Di Pietro A, Falson P: ABCG2 transports and transfers heme to albumin through its large extracellular loop. J Biol Chem. 2010 Oct 22;285(43):33123-33. doi: 10.1074/jbc.M110.139170. Epub 2010 Aug 12. [20705604 ]
  3. Han I, Jun MS, Kim SK, Kim M, Kim JC: Expression pattern and intensity of protoporphyrin IX induced by liposomal 5-aminolevulinic acid in rat pilosebaceous unit throughout hair cycle. Arch Dermatol Res. 2005 Nov;297(5):210-7. Epub 2005 Nov 11. [16231146 ]
  4. Schumacher A, Wafula PO, Teles A, El-Mousleh T, Linzke N, Zenclussen ML, Langwisch S, Heinze K, Wollenberg I, Casalis PA, Volk HD, Fest S, Zenclussen AC: Blockage of heme oxygenase-1 abrogates the protective effect of regulatory T cells on murine pregnancy and promotes the maturation of dendritic cells. PLoS One. 2012;7(8):e42301. doi: 10.1371/journal.pone.0042301. Epub 2012 Aug 10. [22900010 ]


General function:
Involved in oxidoreductase activity
Specific function:
Desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction.
Gene Name:
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Molecular weight:
General function:
Involved in oxidoreductase activity
Specific function:
Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.
Gene Name:
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Molecular weight:
General function:
Involved in oxidoreductase activity
Specific function:
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5.
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Molecular weight: