Ferrochelatase

Ferrochelatase
	Existing structural data: s. UniProt
Properties of human protein
Mass / length primary structure	369 amino acids
Secondary to quaternary structure	Homodimer
Cofactor	(2Fe-2S)
Identifier
Gene name	FECH
External IDs	OMIM : 612386 ; UniProt : P22830 ;
Enzyme classification
EC, category	4.99.1.1 , lyase
Response type	elimination
Substrate	Protoporphyrin IX + Fe 2+
Products	Heme b + 2 H +
Occurrence
Parent taxon	Creature
	Orthologue

Ferrochelatase (also: heme synthase) is an enzyme in eukaryotes and most bacteria , the last step of the synthesis of heme , the chelation of protoporphyrin IX with an iron -II-ion catalyzed . Since the reaction in eukaryotes takes place in the mitochondria or chloroplasts , protoporphyrin must first be transported into these compartments; the exact course of the transport is still unclear. In humans cause mutations on FECH - gene to Ferrochelatasemangel which for the rare hereditary disease erythropoietic Protoporphyrie is responsible. The iron-chelating enzyme has not yet been identified in archaea and sulfate-reducing bacteria , which produce heme using an alternative synthetic route.

Catalyzed reaction

+ Fe ²⁺ ⇔ + 2H ⁺

Protoporphyrin IX is chelated with iron II, protons are split off, and heme b is formed. Conversely, the enzyme can also catalyze the removal of the metal ion during the breakdown of various hems. An iron-sulfur cluster acts as a cofactor . Recombinant ferrochelatase is also able to chelate other divalent metal ions such as cobalt , nickel , zinc or copper .

Individual evidence

↑ ^a ^b BRENDA entry
↑ Jassal, D'Eustachio / reactome: Protoporphyrin IX is transported from the mitochondrial intermembrane space into the mitochondrial matrix ( page no longer available , search in web archives ) Info: The link was automatically marked as defective. Please check the link according to the instructions and then remove this notice. @1@ 2Template: Dead Link / www.reactome.org .
↑ UniProt P22830
↑ M. Kühner et al. : The Alternative Route to Heme in the Methanogenic Archaeon Methanosarcina barkeri . In: Archaea . 2014, 2014. doi : 10.1155 / 2014/327637 .
↑ S. Taketani, M. Ishigaki, A. Mizutani, et al. : Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins . In: Biochemistry . 46, No. 51, December 2007, pp. 15054-61. doi : 10.1021 / bi701460x . PMID 18044970 .
↑ Hunter GA, Sampson MP, Ferreira GC: Metal ion substrate inhibition of ferrochelatase . In: J. Biol. Chem. . 283, No. 35, August 2008, pp. 23685-91. doi : 10.1074 / jbc.M803372200 . PMID 18593702 .

Web links

Wikibooks: Biochemistry and Pathobiochemistry: Porphyrin Biosynthesis - Learning and Teaching Materials

Jassal, D'Eustachio / reactome: Ferrous iron is inserted into protoporphyrin IX to form heme

[b-1] BRENDA entry

[2] Jassal, D'Eustachio / reactome: Protoporphyrin IX is transported from the mitochondrial intermembrane space into the mitochondrial matrix ( page no longer available , search in web archives ) Info: The link was automatically marked as defective. Please check the link according to the instructions and then remove this notice. @1@ 2Template: Dead Link / www.reactome.org .

[3] UniProt P22830

[4] M. Kühner et al. : The Alternative Route to Heme in the Methanogenic Archaeon Methanosarcina barkeri . In: Archaea . 2014, 2014. doi : 10.1155 / 2014/327637 .

[5] S. Taketani, M. Ishigaki, A. Mizutani, et al. : Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins . In: Biochemistry . 46, No. 51, December 2007, pp. 15054-61. doi : 10.1021 / bi701460x . PMID 18044970 .

[6] Hunter GA, Sampson MP, Ferreira GC: Metal ion substrate inhibition of ferrochelatase . In: J. Biol. Chem. . 283, No. 35, August 2008, pp. 23685-91. doi : 10.1074 / jbc.M803372200 . PMID 18593702 .