1.16.3.1: ferroxidase
This is an abbreviated version!
For detailed information about ferroxidase, go to the full flat file.
Word Map on EC 1.16.3.1
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1.16.3.1
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transferrin
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hemoglobin
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anemia
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women
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overload
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children
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c-reactive
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albumin
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erythrocyte
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marrow
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hematological
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pregnancy
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hepcidin
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erythropoietin
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hematocrit
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dialysis
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hereditary
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infant
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spleen
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hemodialysis
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ferric
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thalassemia
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covid-19
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iron-deficient
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ferrous
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fever
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haptoglobin
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corpuscular
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reticulocyte
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admitted
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iron-binding
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micronutrient
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folate
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admission
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wilson
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creatinine
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fibrinogen
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transfusions
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demographic
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beta-thalassemia
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bilirubin
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sickle
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transfused
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acute-phase
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coronavirus
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protoporphyrin
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anthropometric
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d-dimer
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deferoxamine
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biotechnology
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analysis
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hemoglobinopathy
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nutrition
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medicine
- 1.16.3.1
- transferrin
- hemoglobin
- anemia
- women
- overload
- children
-
c-reactive
- albumin
- erythrocyte
- marrow
- hematological
- pregnancy
- hepcidin
- erythropoietin
-
hematocrit
- dialysis
- hereditary
- infant
- spleen
-
hemodialysis
-
ferric
- thalassemia
- covid-19
-
iron-deficient
-
ferrous
- fever
- haptoglobin
-
corpuscular
- reticulocyte
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admitted
-
iron-binding
-
micronutrient
- folate
-
admission
- wilson
- creatinine
- fibrinogen
- transfusions
-
demographic
- beta-thalassemia
- bilirubin
-
sickle
-
transfused
-
acute-phase
- coronavirus
- protoporphyrin
-
anthropometric
-
d-dimer
- deferoxamine
- biotechnology
- analysis
- hemoglobinopathy
- nutrition
- medicine
Reaction
4 Fe(II)
+
4 H+
+
Synonyms
AfFtn, apoferritin, bacterial ferritin, bacterial ferroxidase, bacterioferritin, bacterioferritin B, BFR, BfrB, blue copper oxidase, caeruloplasmin, ceruloplasmin, Cp115, Cp135, Cp200, CT1740, CtFtn, cyto-FOX, cytosolic FOX, DdBfr, Dpr, Dps, Dps protein, Dps-like peroxide resistance protein, Dps-Te, DpsA, DpsA-Te, DspA, EncA, encapsulin, encapsulin A, ferritin, ferro-O2-oxidoreductase, ferro:O2 oxidoreductase, ferroxidase, ferroxidase center of bacterioferritin, ferroxidase I, ferroxidase II, ferroxidase, iron II:oxygen oxidoreductase, Fet3, FET3 gene product, fet3p, FOX1, Ftn, FtnA, H ferritin, H' ferritin, H-chain ferritin, Helicobacter pylori neutrophil-activating protein, hephaestin, HP-NAP, HuHF, human ceruloplasmin form I, human H ferritin, human H-chain ferritin, iron(II): oxygen oxidoreductase, L-ferritin, M ferritin, MaDps, MCO1, MmcO, mnxDEFG, monophenol-o-monoxygenase, More, mouse ceruloplasmin, multicopper ferroxidase, multicopper oxidase, multicopper oxidase 1, multicopper oxidase CueO, multicopper oxidase-1, mushroom tyrosinase, mycobacterial multicopper oxidase, neutrophil-activating protein, non-ceruloplasmin ferroxidase, non-specific DNA-binding protein Dps/ferroxidase, rhHp, rHuHF, Rv0846c, serum ferroxidase, VcDps, VCE_000308, xanthine oxidoreductase
ECTree
1.16.3.1 ferroxidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.16.3.1 - ferroxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
catechol + O2
?
-
mushroom tyrosinase is able to catalyse the oxidation of Fe2+ to Fe3+
-
-
?
N-ethyl-N-2(S-methylsulfonamido)-ethyl-p-phenylenediamine + Fe2+ + O2
?
-
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
-
-
-
?
4 Fe(II) + 4 H+ + O2
4 Fe(III) + 2 H2O
Chlorobaculum tepidum ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
recombinant Chlorobium tepidum ferritin is able to oxidize iron using ferroxidase activity
-
-
?
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
-
-
?
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
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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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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
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
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
-
-
?
Fe(II) + H+ + O2
Fe(III) + H2O
kinetic studies and determination of rate constants at various steps
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-
?
Fe2+ + H+ + O2
Fe3+ + H2O
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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
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-
?
Fe2+ + H+ + O2
Fe3+ + H2O
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multicopper oxidase essential for normal iron homeostasis
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-
?
Fe2+ + H+ + O2
Fe3+ + H2O
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-
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?
N,N'-dimethyl-p-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
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-
-
-
?
p-phenylenediamine + Fe2+ + O2
?
-
no p-phenylenediamine oxidase activity by ferroxidase II
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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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-
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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Acidomyces acidophilus 26774
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
-
-
?
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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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
?
-
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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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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
?
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Helicobacter pylori YS39
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the neutrophil-activating protein has a di-nuclear ferroxidase center and shows ferroxidase activity
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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
?
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ferroxidase II does not catalyze the oxidation of benzylamine
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-
?
additional information
?
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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
?
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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
?
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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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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
?
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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
?
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-
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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-
?
