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Statements

Subject Item
dbr:Protoporphyrin_IX
dbo:wikiPageWikiLink
dbr:Chelatase
Subject Item
dbr:Ligase
dbo:wikiPageWikiLink
dbr:Chelatase
Subject Item
dbr:Cofactor_F430
dbo:wikiPageWikiLink
dbr:Chelatase
Subject Item
dbr:Chelatase
rdfs:label
Chelatase
rdfs:comment
In biochemistry, chelatases are enzymes that catalyze the insertion ("metalation") of naturally occurring tetrapyrroles. Many tetrapyrrole-based cofactors exist in nature including hemes, chlorophylls, and vitamin B12. These metallo cofactors are derived by the reaction of metal cations with tetrapyrroles, which are not ligands per se, but the conjugate acids thereof. In the case of ferrochelatases, the reaction that chelatases catalyze is: Fe2+ + H2P → FeP + 2 H+ In the above equation H2P represents a sirohydrochlorin or a porphyrin, such as protoporphyrin IX.
foaf:depiction
n12:Protoporphyrin_IX.svg
dcterms:subject
dbc:Organometallic_chemistry dbc:Ligases
dbo:wikiPageID
55658980
dbo:wikiPageRevisionID
1120055520
dbo:wikiPageWikiLink
dbr:Biochemistry dbc:Ligases n6:Protoporphyrin_IX.svg dbr:Macrocyclic_ligand dbr:Tetrapyrrole dbr:Chlorophyll dbr:Ligand dbr:Ferrochelatase dbr:Protoporphyrin_IX dbr:Enzyme dbr:Vitamin_B12 dbr:Magnesium_chelatase dbr:Cofactor_(biochemistry) dbr:Cobalt_chelatase dbr:Metalation dbc:Organometallic_chemistry dbr:Heme dbr:Cofactor_F430 dbr:Sirohydrochlorin
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dbt:Enzymes dbt:Short_description
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n12:Protoporphyrin_IX.svg?width=300
dbo:abstract
In biochemistry, chelatases are enzymes that catalyze the insertion ("metalation") of naturally occurring tetrapyrroles. Many tetrapyrrole-based cofactors exist in nature including hemes, chlorophylls, and vitamin B12. These metallo cofactors are derived by the reaction of metal cations with tetrapyrroles, which are not ligands per se, but the conjugate acids thereof. In the case of ferrochelatases, the reaction that chelatases catalyze is: Fe2+ + H2P → FeP + 2 H+ In the above equation H2P represents a sirohydrochlorin or a porphyrin, such as protoporphyrin IX. Chelatases are required because porphyrins and related macrocyclic ligands are extremely slow to metalate, despite favorable thermodynamics. These low rates are attributed to the tight fit of the metal into the rigid 18- or 17-membered tetrapyrrole macrocycle. Several families of chelatase are known including cobalt chelatase, magnesium chelatase, and ferrochelatase. Nickel insertion into a sirohydrochlorin also requires a chelatase as part of the biosynthesis of cofactor F430. Apparently that chelatase is identical to the cobalt chelatase.
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wikipedia-en:Chelatase?oldid=1120055520&ns=0
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2540
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wikipedia-en:Chelatase
Subject Item
dbr:Transition_metal_porphyrin_complexes
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dbr:Chelatase
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dbr:Porphyrin
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dbr:Chelatase
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wikipedia-en:Chelatase
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dbr:Chelatase