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4.98.1.1: protoporphyrin ferrochelatase

This is an abbreviated version!
For detailed information about protoporphyrin ferrochelatase, go to the full flat file.

Word Map on EC 4.98.1.1

Reaction

protoheme
+ 2 H+ =
protoporphyrin
 +
Fe2+

Synonyms

chelatase, ferro-, EC 4.99.1.1, FC1, FC2, FeC, FeCH, ferro-protoporphyrin chelatase, ferrochelatase, ferrochelatase 1, ferrochelatase I, ferrochelatase II, frataxin, HEM15, heme synthase, heme synthetase, hemH, HemH1, HemH2, hFC, host red cell ferrochelatase, iron chelatase, parasite genome-coded ferrochelatase, PfFC, PPIX ferrochelatase, protohaem ferrolyase, protoheme ferro-lyase, protoheme ferrolyase, protoheme lyase, protoporhyrin IX ferrochelatase, protoporphyrin (IX) ferrochelatase, protoporphyrin IX ferrochelatase, Shew_1140, Shew_2229, type II ferrochelatase

ECTree

     4 Lyases
         4.98 ATP-independent chelatases
             4.98.1 Forming coordination complexes
                4.98.1.1 protoporphyrin ferrochelatase

Crystallization

Crystallization on EC 4.98.1.1 - protoporphyrin ferrochelatase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of wild-type and mutants H183A, H88A and K87A with iron, by addition of solid (NH4)2Fe(SO4)2 x 6 H2O, 1.2 A to 1.7 A resolution
in complex with N-methylmesoporphyrin, with and without Cu2+
Mg2+ is required for the formation of Bacillus subtilis ferrochelatase crystals
overview
structure in presence of iron. Only a single iron ion is found in the active site, coordinated in a square pyramidal fashion by two amino acid residues, His183 and Glu264, and three water molecules. This iron ion is not present in the structure of a His183Ala modified ferrochelatase. Insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264
wild-type and mutants Y13F and H183C with N-methyl mesoporphyrin
by the hanging drop method, crystals of mutant E343K with the substrate protoporphyrin IX and mutant R115L without bound substrate. Enzyme with porphyrin bound possesses a significantly more closed active site conformation. In the substrate-bound form, the jaws of the active site mouth are closed so that the porphyrin substrate is completely engulfed in the pocket
crystals of wild-type enzyme in the presence of ammonium chloride or manganese chloride, wild-type enzyme adopts a predominantly open conformation
-
H263C, H341C and F337A mutants, to 2.2 A resolution
mutant enzymes E343D and E343Q in the presence of cobalt chloride, hanging drop vapor diffusion method, using 0.1 M Bis-Tris pH 6.5, 0.05 M ammonium sulfate and a range of pentaerythritol ethoxylate (15/4 EO/OH) varying from 20% to 35% (w/v)
quantum mechanical/molecular mechanics studies. The ferrous iron probably coordinates with residue Met76 at the binding site, and His263 plays the role of proton acceptor. The rate-determining step is either the first proton removed by His263 or the proton transition within the porphyrin with an energy barrier of 14.99 or 14.87 kcal/mol, respectively
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
free form, in complex with Co(II) and in complex with Cd(II) and Hg(I)
in complex with beta-NAD+
-