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Protoporphyrinogen IX

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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).

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

[edit]

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

 
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
 
+ 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]

 
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
 


References

[edit]
  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.