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2-chloro-p-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
2-methoxy-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-methyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-nitro-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
2-sulfonic acid-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
3,4-dihydroxyphenethylamine + Fe2+ + O2
?
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
4 Mn(II) + 4 H+ + O2
4 Mn(III) + 2 H2O
-
-
-
-
?
4 Mn(III) + 4 H+ + O2
4 Mn(IV) + 2 H2O
-
-
-
-
?
4-methylcatechol + Fe2+ + O2
?
-
-
-
-
?
4-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
5-hydroxyindol-3-ylacetic acid + Fe2+ + O2
?
-
-
-
-
?
5-hydroxytryptamine + Fe2+ + O2
?
-
-
-
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?
5-hydroxytryptophan + Fe2+ + O2
?
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-
-
-
?
5-hydroxytryptophol + Fe2+ + O2
?
-
-
-
-
?
alimemazine + Fe2+ + O2
?
-
-
-
-
?
apotransferrin + Fe2+
holotransferrin + ?
apotransferrin + Fe2+ + O2
diferric transferrin + H2O
-
-
-
-
?
catechol + O2
?
-
mushroom tyrosinase is able to catalyse the oxidation of Fe2+ to Fe3+
-
-
?
chlorpromazine + Fe2+ + O2
?
-
-
-
-
?
diethazine + Fe2+ + O2
?
-
-
-
-
?
durenediamine + Fe2+ + O2
?
-
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
Fe(II) + H+ + O2
Fe(III) + H2O
Fe(II) + hydroquinone + O2
Fe(III) + ? + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
ferrous ammonium sulfate + O2
?
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-
-
-
?
ferrous ammonium sulfate + O2
? + H2O
-
-
-
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?
fluphenazine + Fe2+ + O2
?
-
-
-
-
?
hydroquinone + Fe2+ + O2
?
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
L-norepinephrine + Fe2+ + O2
?
-
-
-
-
?
m-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
monophenol + O2
catechol + H2O
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
N,N,N',N'-tetramethyl-p-phenylenediamine + Fe2+
?
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-
-
-
?
N,N-diethyl-p-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
N,N-dimethyl-m-phenylenediamine + Fe2+ + O2
?
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-
-
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?
N,N-dimethyl-p-phenylenediamine + Fe2+ + O2
?
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-
-
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?
N-(p-methoxyphenyl)-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N-acetyl-p-phenylenediamine + Fe2+ + O2
?
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-
-
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?
N-ethyl-N-(2-hydroxyethyl)-p-phenylenediamine Fe2+ + O2
?
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-
-
-
?
N-ethyl-N-(2-hydroxyethyl)p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
r
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
N-phenyl-p-phenylenediamine + Fe2+ + O2
?
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-
-
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?
NADH + O2
NAD+ + H2O
-
-
-
-
?
o-aminophenol + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
o-phenylenediamine + Fe2+ + O2
?
p-aminophenol + Fe2+ + O2
?
-
-
-
-
?
p-anisidine + Fe2+ + O2
?
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?
p-phenylenediamine + Fe2+ + O2
?
periciazine + Fe2+ + O2
?
-
-
-
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?
perphenazine + Fe2+ + O2
?
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?
prochlorperazine + Fe2+ + O2
?
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-
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?
promazine + Fe2+ + O2
?
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-
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?
prometazine + Fe2+ + O2
?
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?
pyrogallol + Fe2+ + O2
?
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?
quinone + Fe2+ + O2
?
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?
thioridazine + Fe2+ + O2
?
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?
trifluoperazine + Fe2+ + O2
?
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?
triflupromazine + Fe2+ + O2
?
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?
additional information
?
-
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
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-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
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-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
similar kinetic activity towards Cu+ as substrate
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the stoichiometry of Fe(II), ferroxldase, and oxygen is 4:1:1
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
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-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
two Fe2+ ions occupy sites Fe1 and Fe2 in the ferroxidase cavity, structure overview
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
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-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
similar kinetic activity towards Cu+ as substrate. The ferroxidase and cuprous oxidase activities are due to the same electron transfer site on the enzyme
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
similar kinetic activity towards Cu+ as substrate. The ferroxidase and cuprous oxidase activities are due to the same electron transfer site on the enzyme
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
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-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
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?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
-
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?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
-
-
-
-
?
4 Fe2+ + 4 H+ + O2
4 Fe3+ + 2 H2O
Thermosynechococcus vestitus
-
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?
apotransferrin + Fe2+
holotransferrin + ?
-
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?
apotransferrin + Fe2+
holotransferrin + ?
-
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?
apotransferrin + Fe2+
holotransferrin + ?
-
-
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?
apotransferrin + Fe2+
holotransferrin + ?
-
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-
-
?
ascorbate + Fe2+ + O2
?
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-
-
-
?
ascorbate + Fe2+ + O2
?
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-
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?
catechol + Fe2+ + O2
?
-
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-
-
?
catechol + Fe2+ + O2
?
-
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
-
-
-
?
Fe(II) + 4 H+ + O2
Fe(III) + 2 H2O
-
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
-
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
kinetic studies and determination of rate constants at various steps
-
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?
Fe(II) + H+ + O2
Fe(III) + H2O
-
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-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
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?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
437996, 437997, 437998, 438000, 438001, 438002, 438003, 438004, 438005, 438006, 438007, 438008, 438009, 438010, 438011, 438012, 438013, 438014, 438015, 438016, 438017, 438020, 438021, 438022, 438024, 438026, 438027, 438028, 438029, 438030, 438032 -
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
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?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
multicopper oxidase essential for normal iron homeostasis
-
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?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
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?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
-
-
-
?
Fe2+ + H+ + O2
Fe3+ + H2O
-
iron acquisition pathway
-
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?
Fe2+ + H+ + O2
Fe3+ + H2O
-
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-
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?
L-epinephrine + Fe2+ + O2
?
-
-
-
-
?
L-epinephrine + Fe2+ + O2
?
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
-
-
-
-
?
o-dianisidine + Fe2+ + O2
?
-
-
-
-
?
o-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
o-phenylenediamine + Fe2+ + O2
?
-
-
-
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?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
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?
p-phenylenediamine + Fe2+ + O2
?
-
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-
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?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
no p-phenylenediamine oxidase activity by ferroxidase II
-
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?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
additional information
?
-
AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid
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?
additional information
?
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-
AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid
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?
additional information
?
-
AaMco1 has ferroxidase activity. AaMco1 is also able to oxidize the N,N-dimethyl-pphenylenediamine dihydrochloride (DMPPDA) compound. Ferroxidase activity of the purified protein is measured by the ferrozine assay. No activity with 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol, and 2-L-ascorbic acid
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?
additional information
?
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-
possesses superoxide dismutase activity
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?
additional information
?
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-
Mn oxidation from soluble Mn(II) to Mn(IV) oxides is a two-step reaction catalyzed by an MCO-containing complex
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?
additional information
?
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-
possesses superoxide dismutase activity
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?
additional information
?
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the Fe-uptake proteins Fet31 and Fet34 support a mechanism of Fe-trafficking that involves channelling of the CaFet34-generated Fe3+ directly to CaFtr1 for transport into the cytoplasm
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?
additional information
?
-
-
enzymatic activity of sFet34 towards ferrous iron is determined by quantifying the velocity of O2 uptake using standard O2-electrode protocols
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?
additional information
?
-
-
-
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?
additional information
?
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only ceruloplasmin capable of complete reoxidation by oxygen
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?
additional information
?
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the non-heme iron-containing ferritin has dual ferroxidase and DNA-binding activities, overview
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?
additional information
?
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-
the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity
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?
additional information
?
-
-
the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity
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?
additional information
?
-
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-
-
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?
additional information
?
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-
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?
additional information
?
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multifunctional protein, copper transport, molecule directly involved in iron mobilization to the plasma by means of its ferroxidase activity, regulator of circulating biogenic amine levels through its oxidase activity
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?
additional information
?
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-
caeruloplasmin inhibits lipid peroxidation and deoxyribose degradation stimulated by iron and copper salts
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?
additional information
?
-
-
ferroxidase II does not catalyze the oxidation of benzylamine
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?
additional information
?
-
-
possesses superoxide dismutase activity
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?
additional information
?
-
-
treatment of mouse BV-2 cells and primary microglial cells with ceruloplasmin induces nitric oxide release and inducible NO synthase mRNA expression. Presence of ceruloplasmin increases levels of mRNAs encoding tumor necrosis factor-alpha, interleukin-1beta, cyclooxygenase-2, and NADPH oxidase. Treatment of BV-2 cells and primary microglia with ceruloplasmin induces phosphorylation of p38 MAP kinase. Ceruloplasmin induces nuclear factor kappaB activation, showing a more sustained pattern than seen with bacterial lipopolysaccharide. Ceruloplasmin-stimulated NO induction is significantly attenuated by p38 inhibitor, SB203580, and the nucleare factor kappaB inhibitor SN50. Ceruloplasmin induces secretion of tumor necrosis factor-alpha and prostaglandin E2 in primary microglial cultures
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?
additional information
?
-
enzyme metal binding structure, overview
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?
additional information
?
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enzyme metal binding structure, overview
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?
additional information
?
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development of the classic chromophoric complex FeIIHx(Tar)2 (H2Tar), 4-(2-thiazolylazo)-resorcinol (x = 0-2) as a robust substrate for evaluation of the ferroxidase function of ceruloplasmin and related enzymes. The catalysis can be followed conveniently in real-time by monitoring the solution absorbance at 720 nm, a fingerprint of FeIIHx(Tar)2. The complex is oxidized to its ferric form FeIIIHx(Tar)2. Fe(II) is transferred formally from FeIIHx(Tar)2 to the substrate docking/oxidation (SDO) site(s) in ceruloplasmin, followed by oxidation to product Fe(III) that is trapped again by the ligand. Each Tar ligand in the above bis-complex coordinates the metal center in a meridional tridentate mode involving a pH-sensitive -OH group (pKa >12), and this imposes rapid Fe(II) and Fe(III) transfer kinetics to facilitate the catalytic process. Method evaluation and proposed mechanism, detailed overview
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?
additional information
?
-
-
usage of a kinetic, automated assay to determine the ferroxidase activity of ceruloplasmin. Enzyme ceruloplasmin shows oxidase activity against ferrous ion,which is the natural substrate, as well as polyphenols, and polyamines. The enzyme oxidizes p-phenylenediamine and o-dianisidine, the substrates are used for assay optimization and evaluation, overview
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?
additional information
?
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enzyme is involved in conferring peroxide tolerance to the bacterium
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?
additional information
?
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formation of the diferric-peroxo (DFP) intermediate and of the ferric-oxo products of the ferroxidase reactions
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?
additional information
?
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-
developmental role of enzyme in nervous system organization
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?
additional information
?
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competitive binding with Zn2+
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?
additional information
?
-
both in vitro and in vivo ceruloplasmin is able to form the specific complex with lactoferrin, the cationic transferrin of exocrine secretions and secretory granules of neutrophils
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?
additional information
?
-
both in vitro and in vivo ceruloplasmin is able to form the specific complex with lactoferrin, the cationic transferrin of exocrine secretions and secretory granules of neutrophils
-
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?
additional information
?
-
-
Fet3p is able to catalyze effectively the incorporation of iron onto apotransferrin
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?
additional information
?
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-
Dps proteins oxidize Fe2+ to Fe3+ using 12 ferroxidase centers, each of them located at a dimer interface
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?
additional information
?
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-
Dpr is also able to bind zinc as an oxidation stable replacement for iron, metal complex binding structure, formation of a di-zinc center, a third zinc ion is found on the surface of the protein, overview
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?
additional information
?
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the divalent metal ions Zn2+, Mn2+, Ni2+, Co2+, and Cu2+ all bind to the ferroxidase center similarly to Fe2+, with moderate affinity, while Mg2+ does not. SsDpr is able to bind various metals as substitutes for iron, enzyme-metal complex structure, overview
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?
additional information
?
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?
additional information
?
-
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?
additional information
?
-
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ascorbate oxidase EC 1.10.3.3 activity
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?