Literature summary for 4.98.1.1 extracted from

Medlock, A.E.; Carter, M.; Dailey, T.A.; Dailey, H.A.; Lanzilotta, W.N.
Product release rather than chelation determines metal specificity for ferrochelatase (2009), J. Mol. Biol., 393, 308-319.

Crystallization (Commentary)

Crystallization (Comment)	Organism
vapor diffusion hanging drop, 291 K, 0.05 M ammonium sulfate, 0.1 M Bis-Tris pH 6.5, 20% pentaerythritolethyloxylate, data for crystals obtained with wild-type human ferrochelatase treated with protoporphyrin IX and Hg, 1.6 A resolution; data for crystals obtained with wild-type human ferrochelatase treated with protoporphyrin IX and Cd, 1.8 A resolution, data for crystals obtained with the F110A variant of human ferrochelatase treated with deuteroporphyrin and Mn, 2.0 A resolution, data for crystals obtained with the F110A variant of human ferrochelatase treated with deuteroporphyrin and Ni, 2.20 A resolution	Homo sapiens

Crystallization (Comment)

Organism

vapor diffusion hanging drop, 291 K, 0.05 M ammonium sulfate, 0.1 M Bis-Tris pH 6.5, 20% pentaerythritolethyloxylate, data for crystals obtained with wild-type human ferrochelatase treated with protoporphyrin IX and Hg, 1.6 A resolution; data for crystals obtained with wild-type human ferrochelatase treated with protoporphyrin IX and Cd, 1.8 A resolution, data for crystals obtained with the F110A variant of human ferrochelatase treated with deuteroporphyrin and Mn, 2.0 A resolution, data for crystals obtained with the F110A variant of human ferrochelatase treated with deuteroporphyrin and Ni, 2.20 A resolution

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
F110A	variant of human ferrochelatase	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism
Cd2+	the crystallographic data indicate that the inhibition of ferrochelatase by Cd2+ occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation	Homo sapiens
Hg2+	the crystallographic data indicate that the inhibition of ferrochelatase by Hg2+ occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation	Homo sapiens
Mn2+	the crystallographic data indicate that the inhibition of ferrochelatase by Mn2+ because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation	Homo sapiens
additional information	the inhibitory metals Hg, Cd, and Mn all serve as substrates for the enzyme in that they are inserted into the porphyrin macrocycle. The crystallographic data indicate that the inhibition of ferrochelatase by these metals occurs because the metallated product is poorly released from the enzyme and is not due to a selection mechanism that occurs prior to chelation	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Metals/Ions

Metals/Ions	Comment	Organism
Cd2+	human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Cd2+ into a porphyrin macrocycle	Homo sapiens
Hg2+	human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Hg2+ into a porphyrin macrocycle	Homo sapiens
Mn2+	human ferrochelatase is capable of catalyzing the insertion of the inhibitory metal ion Mn2+ into a porphyrin macrocycle	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
protoporphyrin IX + Fe2+	Homo sapiens	-	protoheme IX + 2 H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P22830	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
deuteroporphyrin + Mn2+	in contrast to protoporphyrin IX, deuteroporphyrin lacks the vinyl groups at the 2- and 4-ring positions, and therefore, it is possible to structurally discriminate enzyme-bound (metallated) deuteroporphyrin from any possible heme (protoheme) carryover from the enzyme preparation	Homo sapiens	? + H+	-	?
deuteroporphyrin + Ni2+	the Ni-deuteroporphyrin structure is distinctly different from the Mn-deuteroporphyrin model, despite the only variation in enzyme preparation being the addition of either Ni or Mn	Homo sapiens	? + H+	-	?
protoporphyrin IX + Fe2+	-	Homo sapiens	protoheme IX + 2 H+	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ferrochelatase	-	Homo sapiens