15489-90-4

Dark crystals with metalic luster

Crystallise it from pyridine. Dry it at 40o in vacuo.[Beilstein 26 III/IV 3047.]

Hematin is a hydroxide of heme. It may be used to tre at acute porphyric attacks. Hematin suppresses the hepatic aminolevulinic acid (ALA) function and replenishes cytochrome action by restoring the endogenous heme deficit. Early administration of hematin can prevent irreversible neuronal damage induced due to metabolic disorders.

Heme synthesis involves a seven-step enzymatic pathway, commencing with the condensation of glycine and succinyl-CoA to form δ-aminolevulinic acid (ALA). Subsequently, ALA is converted into porphyrinogen (PBG), which is further transformed into porphyrin IX. Ultimately, porphyrin IX binds with iron to form haem. The initial steps of this process occur within the mitochondria, whilst subsequent reactions take place in the cytoplasm. The specific steps are as follows:
(1) Condensation of Glycine and Succinyl-CoA (Enzyme: ALA synthase)
Reaction: Glycine + Succinyl-CoA → δ-aminolevulinic acid (ALA)
(2) Formation of Porphobilinogen (PBG) (Enzyme: ALA dehydratase)
Reaction: 2 ALA → PBG + 2 H2O
(3) Conversion of Porphobilinogen to Uroporphyrinogen III (Enzyme: Porphobilinogen deaminase)
Reaction: 4 PBG → Hydroxymethylbilane + 3 H2O
(4) Decarboxylation of Uroporphyrinogen III (Enzyme: Uroporphyrinogen decarboxylase)
Reaction: Hydroxymethylbilane → Uroporphyrinogen III + CO2 + H2O
(5) Oxidative Decarboxylation of Coproporphyrinogen III (Enzyme: Coproporphyrinogen oxidase)
Reaction: Coproporphyrinogen III → Protoporphyrinogen IX + CO2 + 2H2O
(6) Conversion of Protoporphyrinogen IX to Protoporphyrin IX  (Enzyme: Protoporphyrinogen oxidase)
Reaction: Protoporphyrinogen IX → Protoporphyrin IX + H2O
(7) Insertion of Iron into Protoporphyrin IX (Enzyme: Ferrochelatase)
Reaction: Protoporphyrin IX + Fe2+ → Heme

Store at -20°C