Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4-disulfonic deuteroporphyrin + Fe2+
?
-
-
-
?
Cd2+-protoporphyrin + H+
protoporphyrin + Cd2+
-
poor substrate
-
-
?
Co2+-protoporphyrin + H+
protoporphyrin + Co2+
-
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
deuteroporphyrin + Fe2+
protoheme + H+
-
-
-
-
-
deuteroporphyrin + Mn2+
? + H+
-
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
-
-
?
deuteroporphyrin + Ni2+
? + H+
-
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
-
-
?
deuteroporphyrin IX + Zn2+
Zn deuteroporphyrin IX + H+
-
in vitro, zinc is the preferred substrate at all concentrations of porphyrin
-
-
?
deuteroporphyrin IX + Zn2+
Zn-deuteroporphyrin IX + H+
Fe2+-2,4-bis-acetal deuteroporphyrin
?
-
-
-
-
?
Fe2+-2,4-diacetyldeuteroporphyrin
?
-
-
-
-
?
Fe2+-2,4-disulfonate deuteroporphyrin
?
-
-
-
-
?
Fe2+-mesoporphyrin IX + H+
mesoporphyrin IX + Fe2+
-
-
-
-
?
Fe2+-protoporphyrin + H+
protoporphyrin + Fe2+
-
-
-
-
?
heme + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
hemin + H+
mesoporphyrin IX + Zn2+
-
-
-
-
r
hemoglobin + Zn2+
Zn-protoporphyrin + H+
mesoporphyrin + Fe2+
mesoheme
pH 8.0
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
mesoporphyrin + Zn2+
mesoheme
-
37°C
-
-
?
mesoporphyrin + Zn2+
Zn-mesoporphyrin + H+
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
mesoporphyrin IX + Fe2+
mesoheme IX + H+
mesoporphyrin IX + Fe2+
protoporphyrin IX + H+
-
-
-
-
?
mesoporphyrin IX + ferrous ammonium sulfate
mesoheme + ammonium sulfate
-
room temperature
-
-
?
mesoporphyrin IX + Zn2+
hemin + H+
-
-
-
-
r
myoglobin + Zn2+
Zn-protoporphyrin + H+
N-methyl mesoporphyrin + Cu2+
?
-
pH 7.4
-
-
?
N-methyl mesoporphyrin + Zn2+
?
-
pH 7.4
-
-
?
porphyrin + Fe2+
heme + H+
-
-
-
-
?
porphyrin + metal ion
metalloporphyrin
protoheme + H+
protoporphyrin + Fe2+
protoporphyrin + Cu2+
Cu2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
protoporphyrin + Fe2+
protoheme + H+
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
protoporphyrin IX + Co2+
?
-
-
-
-
?
protoporphyrin IX + Co2+
Co2+-protoporphyrin + H+
-
-
-
-
?
protoporphyrin IX + Cu2+
?
-
-
-
-
?
protoporphyrin IX + Cu2+
Cu2+-protoporphyrin + H+
-
Cu2+ is a good substrate
-
-
?
protoporphyrin IX + Fe2+
?
protoporphyrin IX + Fe2+
heme + H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + H+
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
protoporphyrin IX + Fe2+
protoheme IX + H+
protoporphyrin IX + FeCl3
protoheme + HCl
pH 7.5, 37°C
-
-
-
protoporphyrin IX + Ni2+
?
-
-
-
-
?
protoporphyrin IX + Zn2+
?
protoporphyrin IX + Zn2+
Zn protoporphyrin IX
-
pH 7.4, room temperature
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX + H+
-
-
-
-
?
protoporphyrin IX + Zn2+
Zn2+-protoporphyrin IX + H+
-
-
-
-
?
Sn2+-protoporphyrin + H+
protoporphyrin + Sn2+
-
-
-
-
?
Zn2+-mesoporphyrin + H+
mesoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
protoporphyrin + Zn2+
additional information
?
-
deuteroporphyrin + Fe2+

deuteroheme + H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
?
deuteroporphyrin + Fe2+
deuteroheme + H+
-
-
-
?
deuteroporphyrin IX + Zn2+

Zn-deuteroporphyrin IX + H+
-
-
-
-
?
deuteroporphyrin IX + Zn2+
Zn-deuteroporphyrin IX + H+
-
-
-
-
?
Fe2+-hematoporphyrin

?
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
Fe2+-hematoporphyrin
?
-
-
-
-
?
hemoglobin + Zn2+

Zn-protoporphyrin + H+
-
-
-
-
?
hemoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
hemoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
mesoporphyrin + Fe2+

mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
-
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
-
?
mesoporphyrin + Fe2+
mesoheme + H+
-
-
-
?
mesoporphyrin IX + Fe2+

?
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+
?
-
-
-
-
?
mesoporphyrin IX + Fe2+

mesoheme IX + H+
-
-
-
-
?
mesoporphyrin IX + Fe2+
mesoheme IX + H+
-
-
-
-
?
myoglobin + Zn2+

Zn-protoporphyrin + H+
-
-
-
-
?
myoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
myoglobin + Zn2+
Zn-protoporphyrin + H+
-
-
-
-
?
porphyrin + metal ion

metalloporphyrin
-
Fe2+, Zn2+, Co2+
-
-
?
porphyrin + metal ion
metalloporphyrin
-
-
-
?
porphyrin + metal ion
metalloporphyrin
-
Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
?
porphyrin + metal ion
metalloporphyrin
-
Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
?
porphyrin + metal ion
metalloporphyrin
-
Co2+, Fe2+, Zn2+, Ni2+ or Mn2+
-
-
?
protoheme + H+

protoporphyrin + Fe2+
-
-
-
-
?
protoheme + H+
protoporphyrin + Fe2+
-
-
-
-
r
protoporphyrin + Fe2+

protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 to facilitate mitochondrial ferrous iron transfer for erythroid heme biosynthesis
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + 2 H+
-
-
?
protoporphyrin + Fe2+

protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
-
-
-
?
protoporphyrin + Fe2+
protoheme + H+
-
the kcat of the forward reaction is about 11fold higher than the reverse reaction
-
-
r
protoporphyrin + Fe2+
protoheme + H+
-
-
-
?
protoporphyrin + Zn2+

Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
?
protoporphyrin + Zn2+
Zn2+-protoporphyrin + H+
-
-
-
-
?
protoporphyrin IX + Fe2+

?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
insertion of a metal ion into protoporphyrin IX by ferrochelatase occurs from a metal binding site represented by His183 and Glu264
-
-
?
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
-
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+
?
final step of heme biosynthesis
-
-
-
protoporphyrin IX + Fe2+

protoheme + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme + H+
-
pH 7.6, 30°C, unaerobic conditions
-
-
?
protoporphyrin IX + Fe2+
protoheme + H+
pH 8.0, 37°C
-
-
?
protoporphyrin IX + Fe2+
protoheme + H+
-
pH 8.1, 30°C
-
-
-
protoporphyrin IX + Fe2+
protoheme + H+
-
under strictly anaerobic conditions
-
-
?
protoporphyrin IX + Fe2+

protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
the enzymatic product protoheme IX is a well-known cofactor in a wide range of proteins
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + 2 H+
-
-
-
-
?
protoporphyrin IX + Fe2+

protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
enzyme undergoes significant changes in secondary structure during the catalytic cycle
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
substrate is bound deep within an enclosed pocket
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
?
protoporphyrin IX + Fe2+
protoheme IX + H+
-
-
-
-
?
protoporphyrin IX + Zn2+

?
-
-
-
-
?
protoporphyrin IX + Zn2+
?
-
-
-
?
protoporphyrin IX + Zn2+

Zn-protoporphyrin IX
-
-
-
?
protoporphyrin IX + Zn2+
Zn-protoporphyrin IX
pH 8.0, 35°C
-
-
-
Zn2+-mesoporphyrin + H+

mesoporphyrin + Zn2+
-
-
-
-
?
Zn2+-mesoporphyrin + H+
mesoporphyrin + Zn2+
-
-
-
-
?
Zn2+-protoporphyrin + H+

protoporphyrin + Zn2+
-
-
-
-
?
Zn2+-protoporphyrin + H+
protoporphyrin + Zn2+
-
-
-
-
?
additional information

?
-
-
metal substrates are Fe2+, Zn2+, Cu2+, no substrate: Co2+, Fe3+
-
?
additional information
?
-
-
ferric iron is not a substrate
-
-
-
additional information
?
-
-
the enzyme is highly specific for ferrous ion in vivo, however in vitro ferrochelatase catalyzes insertion of a remarkable variety of divalent metal ions into protoporphyrin and other closely related porphyrins
-
-
-
additional information
?
-
-
the enzyme is promiscuous in vitro and can insert Zn2+, Co2+, Cu2+, and Ni2+ into protoporphyrin IX in addition to the physiological substrate Fe2+, however, the insertion of metal ions other than Fe2+ occurs rarely in vivo
-
-
-
additional information
?
-
-
2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
-
-
-
additional information
?
-
-
not: isoporphyrin
-
-
-
additional information
?
-
-
2,4-disulfonic deuteroporphyrin, 2,4-bisglycol deuteroporphyrin
-
-
-
additional information
?
-
-
metal substrates are Fe2+, Zn2+, Co2+
-
?
additional information
?
-
-
frataxin binds at nanomolar affinity to the ferrochelatase and the iron-sulfur cluster assembly apparatus, monomeric frataxin interacts with the ferrochelatase dimer predominantly utilizing frataxinās helical surface, including iron binding residues in the helix-1/strand-1 conserved acidic residue patch of the protein
-
-
-
additional information
?
-
-
ferric iron is not a substrate
-
-
-
additional information
?
-
-
the enzyme is highly specific for ferrous ion in vivo, however in vitro ferrochelatase catalyzes insertion of a remarkable variety of divalent metal ions into protoporphyrin and other closely related porphyrins
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
in wild type and H207N mutant, addition of porphyrin yields a 1:1 complex with protein, in E287Q mutant addition is in in substoichiometric ratio with protein
-
?
additional information
?
-
-
overview on active site and substrate binding
-
?
additional information
?
-
-
the inhibitory metal ion-binding site of ferrochelatase is composed of multiple residues but primarily defined by His-287 and Phe-283 and is crucial for optimal activity at low metal ion concentrations. This binding site may be important for ferrous iron acquisition and desolvation in vivo
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.05 - 0.054
(25R)-3beta-hydroxycholest-5-en-27-oate
0.056
2,4-bisacetal deuteroporphyrin
-
-
0.479
2,4-diacetyldeuteroporphyrin
-
-
0.052
2,4-disulfonic deuteroporphyrin
-
-
0.0213
deuteroporphyrin
-
-
0.0026 - 0.0461
deuteroporphyrin IX
0.055
hematoporphyrin
-
-
0.0057
hemin
-
pH 5.5, 45°C
0.004 - 0.1
mesoporphyrin
0.0047 - 0.0302
mesoporphyrin IX
0.012
myoglobin
-
at pH 6.5 and 30°C
-
0.0121 - 0.0246
porphyrin
0.002 - 0.05
protoporphyrin
0.00022 - 0.72
protoporphyrin IX
0.05
(25R)-3beta-hydroxycholest-5-en-27-oate

-
mutant E272S, in the presence of 4 mM Mg2+, pH 7.4, room temperature
0.054
(25R)-3beta-hydroxycholest-5-en-27-oate
-
mutant E272S, pH 7.4, room temperature
0.0052
Co2+

-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.56
Co2+
-
mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication; pH 7.4, 21°C, mutant enzyme Y13M
0.063
Cu2+

-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.0026
deuteroporphyrin IX

-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.0144
deuteroporphyrin IX
-
pH 7.7, 28°C
0.0461
deuteroporphyrin IX
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.00048
Fe2+

-
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.00108
Fe2+
-
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.00113
Fe2+
-
mutant V251L, pH 8.1, 30°C
0.00146
Fe2+
-
mutant P255R, pH 8.1, 30°C
0.0019
Fe2+
-
wild-type, pH 8.1, 30°C
0.00226
Fe2+
-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0028
Fe2+
-
mutant C341S
0.00291
Fe2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0038
Fe2+
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
0.0039
Fe2+
-
free enzyme, pH 8.0, 30°C
0.0047
Fe2+
-
pH 7.7, 28°C
0.00515
Fe2+
-
mutant S249A/K250Q/V251C, pH 8.1, 30°C
0.006
Fe2+
-
cosubstrate protoporphyrin
0.00728
Fe2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0083
Fe2+
-
mutant M267I, heterodimer, room temperature
0.00895
Fe2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0094
Fe2+
-
M11V/G104A, pH 7.6, 30°C, unaerobic conditions
0.0095
Fe2+
-
presence of CuCl2
0.0098
Fe2+
-
mutant E343D
0.01
Fe2+
-
R31G, pH 7.6, 30°C, unaerobic conditions
0.0114
Fe2+
-
wild-type, heterodimer, room temperature
0.0117
Fe2+
-
mutant M267I, homodimer, room temperature
0.0119
Fe2+
-
wild-type, homodimer, room temperature
0.013
Fe2+
-
wild-type, pH 7.6, 30°C, unaerobic conditions
0.0139
Fe2+
-
mutant C219S
0.014
Fe2+
-
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.0141
Fe2+
-
mutant C236Y, homodimer, room temperature
0.017
Fe2+
-
mutant E61K, pH 7.6, 30°C, unaerobic conditions
0.0177
Fe2+
-
mutant F337A
0.0179
Fe2+
-
mutant C236Y, heterodimer, room temperature
0.019
Fe2+
-
mutant T302A, pH 7.6, 30°C, unaerobic conditions
0.02
Fe2+
-
absence of Cu2+
0.021
Fe2+
-
mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions
0.021
Fe2+
-
mutant R115L
0.0219
Fe2+
-
mutant Q139L, heterodimer, room temperature
0.0232
Fe2+
-
mutant K379N, heterodimer, room temperature
0.0235
Fe2+
-
mutant S264L, heterodimer, room temperature
0.0251
Fe2+
-
mutant Y191H, homodimer, room temperature
0.0262
Fe2+
-
mutant Q139L, homodimer, room temperature
0.0331
Fe2+
-
cosubstrate protoporphyrin
0.0338
Fe2+
-
mutant N75A
0.036
Fe2+
-
cosubstrate mesoporphyrin
0.038
Fe2+
-
mutant Y191H, heterodimer, room temperature
0.0441
Fe2+
-
mutant F260L, heterodimer, room temperature
0.0488
Fe2+
-
mutant P334L, homodimer, room temperature
0.0763
Fe2+
-
mutant F260L, homodimer, room temperature
0.1101
Fe2+
-
mutant K379N, homodimer, room temperature
0.004
mesoporphyrin

-
non-saturating Fe2+ concentration
0.0077
mesoporphyrin
-
mutant H388A, 37°C
0.0085
mesoporphyrin
-
wild-type, 37°C
0.0092
mesoporphyrin
-
mutant H388A, co-expressed with wild-type, 37°C
0.0093
mesoporphyrin
-
mutant C395delta, co-expressed with wild-type, 37°C
0.0105
mesoporphyrin
-
mutant M267I, co-expressed with wild-type, 37°C
0.0111
mesoporphyrin
-
mutant I186T, co-expressed with wild-type, 37°C
0.012
mesoporphyrin
-
mutant H263A, 37°C; mutant H263A, co-expressed with wild-type, 37°C
0.0047
mesoporphyrin IX

-
mutant C341S
0.0061
mesoporphyrin IX
-
mutant M267I, heterodimer, room temperature
0.0066
mesoporphyrin IX
-
pH 8.0, 37°C
0.008
mesoporphyrin IX
-
-
0.0087
mesoporphyrin IX
-
wild-type
0.0089
mesoporphyrin IX
-
-
0.0092
mesoporphyrin IX
-
mutant Q139L, heterodimer, room temperature
0.0094
mesoporphyrin IX
-
wild-type, heterodimer, room temperature
0.0096
mesoporphyrin IX
-
wild-type
0.0097
mesoporphyrin IX
-
mutant F260L, heterodimer, room temperature
0.0121
mesoporphyrin IX
-
wild-type, homodimer, room temperature
0.0123
mesoporphyrin IX
-
mutant M267I, homodimer, room temperature
0.0127
mesoporphyrin IX
-
mutant C219S
0.0129
mesoporphyrin IX
-
mutant C236Y, heterodimer, room temperature; mutant Y191H, homodimer, room temperature
0.0138
mesoporphyrin IX
-
mutant S264L, heterodimer, room temperature
0.0146
mesoporphyrin IX
-
mutant F260L, homodimer, room temperature
0.0172
mesoporphyrin IX
-
mutant Y191H, heterodimer, room temperature
0.0182
mesoporphyrin IX
-
mutant P334L, homodimer, room temperature
0.0224
mesoporphyrin IX
-
mutant K379N, homodimer, room temperature
0.0253
mesoporphyrin IX
-
mutant K379N, heterodimer, room temperature
0.0267
mesoporphyrin IX
-
-
0.0267
mesoporphyrin IX
-
mutant Q139L, homodimer, room temperature
0.0302
mesoporphyrin IX
-
mutant C236Y, homodimer, room temperature
0.02206
Ni2+

-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.03218
Ni2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.06521
Ni2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.1037
Ni2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0121
porphyrin

-
wild-type
0.0123
porphyrin
-
mutant E343D
0.0168
porphyrin
-
mutant N75A
0.0246
porphyrin
-
mutant F337A
0.002
protoporphyrin

-
non-saturating Fe2+ concentration
0.00819
protoporphyrin
-
-
0.009
protoporphyrin
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
0.00935
protoporphyrin
-
-
0.01
protoporphyrin
-
free enzyme, pH 8.0, 30°C
0.0125
protoporphyrin
-
-
0.0127
protoporphyrin
-
-
0.0153
protoporphyrin
-
-
0.0168
protoporphyrin
-
-
0.00022
protoporphyrin IX

wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.00026
protoporphyrin IX
-
wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00029
protoporphyrin IX
-
mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0003
protoporphyrin IX
mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.00044
protoporphyrin IX
-
mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions
0.00078
protoporphyrin IX
-
mutant E61K, pH 7.6, 30°C, unaerobic conditions
0.00079
protoporphyrin IX
-
mutant T302A, pH 7.6, 30°C, unaerobic conditions
0.00083
protoporphyrin IX
-
R31G, pH 7.6, 30°C, unaerobic conditions
0.00086
protoporphyrin IX
-
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.00091
protoporphyrin IX
-
wild-type, pH 7.6, 30°C, unaerobic conditions
0.001
protoporphyrin IX
-
wild type enzyme, at pH 8.0, temperature not specified in the publication
0.00123
protoporphyrin IX
-
mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.0013
protoporphyrin IX
-
M11V/G104A, pH 7.6, 30°C, unaerobic conditions
0.0014
protoporphyrin IX
-
wild-type, under strictly anaerobic conditions
0.0014
protoporphyrin IX
-
wild-type, pH 8.1, 30°C
0.00172
protoporphyrin IX
-
wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00182
protoporphyrin IX
-
mutant V251L, pH 8.1, 30°C
0.00243
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00251
protoporphyrin IX
-
mutant P255G, under strictly anaerobic conditions
0.00265
protoporphyrin IX
-
mutant P255R, under strictly anaerobic conditions
0.00265
protoporphyrin IX
-
mutant P255R, pH 8.1, 30°C
0.005
protoporphyrin IX
-
mutant enzyme F283L, at pH 8.0, temperature not specified in the publication
0.00547
protoporphyrin IX
-
mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00558
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00684
protoporphyrin IX
-
mutant S249A/K250Q/V251C, under strictly anaerobic conditions
0.00684
protoporphyrin IX
-
mutant S249A/K250Q/V251C, pH 8.1, 30°C
0.00831
protoporphyrin IX
-
mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.01034
protoporphyrin IX
-
mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions
0.01034
protoporphyrin IX
-
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.01125
protoporphyrin IX
-
mutant K250M/V251L/W256Y, under strictly anaerobic conditions
0.01125
protoporphyrin IX
-
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.0285
protoporphyrin IX
-
-
0.116
protoporphyrin IX
-
mutant enzyme H287L, at pH 8.0, temperature not specified in the publication
0.72
protoporphyrin IX
-
pH 7.5, 37°C
0.00017
Zn2+

-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.000488
Zn2+
wild type enzyme, at pH 8.0 and 30°C
0.000836
Zn2+
mutant enzyme FeChDELTA347, at pH 8.0 and 30°C
0.0011
Zn2+
-
pH 8.0, 37°C
0.0015
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
0.0095
Zn2+
-
mutant H263A, co-expressed with wild-type, 37°C
0.0105
Zn2+
-
mutant H388A, co-expressed with wild-type, 37°C
0.0108
Zn2+
-
mutant H388A, 37°C
0.011
Zn2+
-
mutant I186T, co-expressed with wild-type, 37°C
0.0114
Zn2+
-
wild-type, 37°C
0.013
Zn2+
-
pH 7.4, 21°C, wild-type enzyme
0.018
Zn2+
-
mutant C395delta, co-expressed with wild-type, 37°C
0.024
Zn2+
-
mutant M267I, co-expressed with wild-type, 37°C
0.024
Zn2+
-
wild-type, in the presence of 4 mM Mg2+, pH 7.4, room temperature
0.04
Zn2+
-
mutant H263A, 37°C
0.055
Zn2+
-
wild-type, pH 7.4, room temperature
0.06
Zn2+
-
at pH 6.5 and 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.065
Cu2+
-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.52
hemin
-
pH 5.5, 45°C
6.7
mesoporphyrin IX
-
pH 8.0, 37°C
0.01167 - 0.0573
porphyrin
0.3 - 1.53
protoporphyrin
0.0125 - 1.9
protoporphyrin IX
0.016
Co2+

-
pH 7.4, 21°C, wild-type enzyme; wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication
0.033
Co2+
-
mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication; pH 7.4, 21°C, mutant enzyme Y13M
0.018
Fe2+

-
wild-type
0.02
Fe2+
-
R31G, pH 7.6, 30°C, unaerobic conditions
0.023
Fe2+
-
wild-type, pH 7.6, 30°C, unaerobic conditions
0.032
Fe2+
-
mutant T302A, pH 7.6, 30°C, unaerobic conditions
0.033
Fe2+
-
mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions
0.038
Fe2+
-
M11V/G104A, pH 7.6, 30°C, unaerobic conditions
0.04
Fe2+
-
mutant E61K, pH 7.6, 30°C, unaerobic conditions
0.05
Fe2+
-
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.053
Fe2+
-
mutant F110A; mutant R115L
0.055
Fe2+
-
E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions
0.063
Fe2+
-
mutant C341S
0.068
Fe2+
-
wild-type, pH 8.1, 30°C
0.13
Fe2+
-
mutant P255R, pH 8.1, 30°C
0.138
Fe2+
-
mutant V251L, pH 8.1, 30°C
0.235
Fe2+
-
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.3
Fe2+
-
mutant S249A/K250Q/V251C, pH 8.1, 30°C
0.01167
porphyrin

-
mutant E343D
0.0135
porphyrin
-
mutant F337A
0.016
porphyrin
-
mutant N75A
0.0573
porphyrin
-
wild-type
0.3 - 0.483
protoporphyrin

-
-
1.51
protoporphyrin
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
1.53
protoporphyrin
-
free enzyme, pH 8.0, 30°C
0.0125
protoporphyrin IX

-
wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.013
protoporphyrin IX
-
pH 7.5, 37°C
0.05
protoporphyrin IX
-
mutant K250M/V251L/W256Y, pH 8.1, 30°C
0.051
protoporphyrin IX
-
mutant K250M/V251L/W256Y, under strictly anaerobic conditions
0.052
protoporphyrin IX
wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.068
protoporphyrin IX
-
wild-type, under strictly anaerobic conditions
0.068
protoporphyrin IX
-
wild-type, pH 8.1, 30°C
0.0683
protoporphyrin IX
-
wild-type
0.073
protoporphyrin IX
mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C
0.098
protoporphyrin IX
-
mutant P255G, under strictly anaerobic conditions
0.0983
protoporphyrin IX
-
mutant P255G
0.13
protoporphyrin IX
-
mutant P255R, under strictly anaerobic conditions
0.13
protoporphyrin IX
-
mutant P255R, pH 8.1, 30°C
0.138
protoporphyrin IX
-
mutant V251L, pH 8.1, 30°C
0.142
protoporphyrin IX
-
wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.212
protoporphyrin IX
-
mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.234
protoporphyrin IX
-
mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions
0.235
protoporphyrin IX
-
mutant Q248P/S249G/K250P/G252W, pH 8.1, 30°C
0.3
protoporphyrin IX
-
mutant S249A/K250Q/V251C, under strictly anaerobic conditions
0.3
protoporphyrin IX
-
mutant S249A/K250Q/V251C, pH 8.1, 30°C
0.44
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.59
protoporphyrin IX
-
mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.21
protoporphyrin IX
-
mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.6
protoporphyrin IX
-
mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.9
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.034
Zn2+

wild type enzyme, at pH 8.0 and 30°C
0.049
Zn2+
mutant enzyme FeChDELTA347, at pH 8.0 and 30°C
3.2
Zn2+
-
no added cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
3.5
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
76 - 1200
deuteroporphyrin IX
0.000092
hemin
-
pH 5.5, 45°C
0.00101
mesoporphyrin IX
-
pH 8.0, 37°C
0.018 - 2015
protoporphyrin IX
76
deuteroporphyrin IX

-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
1200
deuteroporphyrin IX
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
62.5
Fe2+

-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
179
Fe2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
261.3
Fe2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
416.8
Fe2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.56
Ni2+

-
wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
1.605
Ni2+
-
mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
4.23
Ni2+
-
mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
9.05
Ni2+
-
mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
150
protoporphyrin

-
free enzyme, pH 8.0, 30°C
170
protoporphyrin
-
in complex with protoporphyrinogen dehydrogenase PgdH1, pH 8.0, 30°C
0.018
protoporphyrin IX

-
pH 7.5, 37°C
47.3
protoporphyrin IX
-
wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
82.3
protoporphyrin IX
-
wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
145.7
protoporphyrin IX
-
mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
173.3
protoporphyrin IX
-
mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
180
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
292.8
protoporphyrin IX
-
mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
340.5
protoporphyrin IX
-
mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
2015
protoporphyrin IX
-
mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C
0.00525
Zn2+

-
pH 8.0, 37°C
2200
Zn2+
-
0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
19000
Zn2+
-
for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.