1.16.3.2: bacterial non-heme ferritin
This is an abbreviated version!
For detailed information about bacterial non-heme ferritin, go to the full flat file.
Word Map on EC 1.16.3.2
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1.16.3.2
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ferroxidase
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nanocage
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iron-storage
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ferritin-like
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apoferritin
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bacterioferritins
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h-chains
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nutrition
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environmental protection
- 1.16.3.2
- ferroxidase
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nanocage
-
iron-storage
-
ferritin-like
- apoferritin
- bacterioferritins
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h-chains
- nutrition
- environmental protection
Reaction
2 Fe(II)
+
Synonyms
bacterial ferritin, bacterioferritin, BFR, BfrB, CjDps, DNA-binding protein from starved cells, Dps protein, DpsA, EcFtnA, ferritin, ferritin A, Ftn, FtnA, HuHF, L-ferritin, M ferritin, non-cytochrome ferritin, non-heme bacterial ferritin, non-heme ferritin, non-heme type bacterial ferritin, nonheme bacterial ferritin, nonheme FtnA
ECTree
1.16.3.2 bacterial non-heme ferritinAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.16.3.2 - bacterial non-heme ferritin
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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
2 Fe(II) + H2O2 + 2 H2O
2 [FeO(OH)] + 4 H+
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?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
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?
2 Fe(II) + O2 + 4 H2O
2 [FeO(OH)] + 4 H+ + H2O2
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?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
overall reaction
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?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
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?
4 Fe(II) + O2 + 6 H2O
4 [FeO(OH)] + 8 H+
overall reaction
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?
additional information
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the formation of the iron hydroxide core is monitored spectrophotometrically at 305 nm. The enzyme is able to bind DNA, DNA-binding analysis fro wild-type and mutant enzymes, overview
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?
additional information
?
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the formation of the iron hydroxide core is monitored spectrophotometrically at 305 nm. The enzyme is able to bind DNA, DNA-binding analysis fro wild-type and mutant enzymes, overview
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?
additional information
?
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although H2O2 is a product of dioxygen reduction in FtnA and oxidation occurs with a stoichiometry of Fe2+/O2 about 3:1 most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe2+/H2O2 stoichiometry, thus suppressing hydroxyl-radical formation
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?
additional information
?
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in addition to the conserved A- and B-sites of the diiron ferroxidase center, EcFtnA has a third iron-binding site (the C-site) that is near the diiron site. The enzyme requires fully functional A- and B-sites for high ferroxidase activity. There are multiple iron-oxidation pathways in EcFtnA with O2 and H2O2 as oxidants. While H2O2 is a product of dioxygen reduction in EcFtnA and oxidation occurs with a stoichiometry of Fe(II)/O2 about 3:1, most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe(II)/H2O2 stoichiometry, thus suppressing hydroxyl radical formation. One of the unique properties of EcFtnA is its unusual Fe(II)/O2 oxidation stoichiometry of approx. 3
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?
additional information
?
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in addition to the conserved A- and B-sites of the diiron ferroxidase center, EcFtnA has a third iron-binding site (the C-site) that is near the diiron site. The enzyme requires fully functional A- and B-sites for high ferroxidase activity. There are multiple iron-oxidation pathways in EcFtnA with O2 and H2O2 as oxidants. While H2O2 is a product of dioxygen reduction in EcFtnA and oxidation occurs with a stoichiometry of Fe(II)/O2 about 3:1, most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe(II)/H2O2 stoichiometry, thus suppressing hydroxyl radical formation. One of the unique properties of EcFtnA is its unusual Fe(II)/O2 oxidation stoichiometry of approx. 3
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?
additional information
?
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in bacterioferritin, iron mineralization kinetics are dependent on an intra-subunit catalytic diiron cofactor site (the ferroxidase centre), three closely located aromatic residues and an inner surface iron site. One of the aromatic residues, Tyr25, is the site of formation of a transient radical. The other two residues are Tyr58 and Trp133, these residues are important for the rates of formation and decay of the Tyr25 radical and decay of a secondary radical observed during Tyr25 radical decay. Mechanism in which these aromatic residues function in electron transfer from the inner surface site to the ferroxidase centre, overview
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?
additional information
?
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addition of 2 Fe2+ ions per subunit or 4 Fe2+ ions per subunit in frog wild-type or H54A mutant M ferritin. Recombinant ferritin protein cages are mineralized with ferrous sulfate, 20 Fe2+ ions per subunit. Fe2+ exit from caged ferritin minerals is initiated by reducing the ferritin mineral with added NADH and FMN and trapping the reduced and dissolved Fe2+ as the [Fe(2,2'-bipyridyl)3]2+ complex outside the protein cage. Fe2+ release from the protein cage is measured as the absorbance of [Fe(2,2'-bipyridyl)3]2+ at the maximum of A522 nm
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