Protoporphyrinogen IX

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Protoporphyrinogen IX
Protoporphyrinogen IX neutral.svg
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
MeSH protoporphyrinogen
PubChem CID
  • InChI=1S/C34H40N4O4/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/h7-8,35-38H,1-2,9-16H2,3-6H3,(H,39,40)(H,41,42)/p-2
    Key: UHSGPDMIQQYNAX-UHFFFAOYSA-L
  • CC1=C2CC3=C(C(=C(N3)CC4=C(C(=C(N4)CC5=C(C(=C(N5)CC(=C1CCC(=O)[O-])N2)CCC(=O)[O-])C)C=C)C)C=C)C
Properties
C34H38N4O4
Molar mass 566.7 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

Protoporphyrinogen IX is an organic chemical compound which is produced along the synthesis of porphyrins, a class of critical biochemicals that include hemoglobin and chlorophyll. It is a direct precursor of protoporphyrin IX.

The compound is a porphyrinogen, meaning that it has a non-aromatic hexahydroporphine core, which will be oxidized to a porphine core in later stages of the heme synthesis. Like most porphyrinogens, it is colorless.[ citation needed ]

Biosynthesis

The compound is synthesized in most organisms from coproporphyrinogen III by the enzyme coproporphyrinogen oxidase: [1]

Coproporphyrinogen III neutral.svg
coproporphyrinogen III
 
O2
2 H2O
Protoporphyrinogen IX
O2
2 H2O
 
Protoporphyrinogen IX neutral.svg
protoporphyrinogen IX
+ 2 CO2
 

The process entails conversion of two of four propionic acid groups to vinyl groups. [2]

By the action of protoporphyrinogen oxidase, protoporphyrinogen IX is later converted into protoporphyrin IX, the first colored tetrapyrrole in the biosynthesis of hemes. [3] [4]

Protoporphyrinogen IX neutral.svg
protoporphyrinogen IX
 
3 O2
3 H2O2
Protoporphyrinogen IX
3 O2
3 H2O2
 
Protoporphyrin IX neutral.svg
protoporphyrin IX

References

  1. ↑ Enzyme 1.3.3.3 at KEGG Pathway Database.
  2. ↑ Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S (October 1993). "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation". The Journal of Biological Chemistry. 268 (28): 21359–63. doi: 10.1016/S0021-9258(19)36931-5 . PMID   8407975.
  3. ↑ Paul R. Ortiz de Montellano (2008). "Hemes in Biology". Wiley Encyclopedia of Chemical Biology. John Wiley & Sons. pp. 1–10. doi:10.1002/9780470048672.wecb221. ISBN   978-0470048672.
  4. ↑ Enzyme 1.3.3.4 at KEGG Pathway Database.


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