Protoporphyrinogen IX

Protoporphyrinogen IX
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
MeSH protoporphyrinogen
  • 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).
Infobox references

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.

Biosynthesis

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

2D representation of the chemical structure of coproporphyrinogen III .
coproporphyrinogen III
 
O2
2 H2O
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
O2
2 H2O
 
2D representation of the chemical structure of protoporphyrinogen IX .
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]

2D representation of the chemical structure of protoporphyrinogen IX .
protoporphyrinogen IX
 
3 O2
3 H2O2
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
3 O2
3 H2O2
 
2D representation of the chemical structure of protoporphyrin IX .
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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