1.15.1.2: superoxide reductase
This is an abbreviated version!
For detailed information about superoxide reductase, go to the full flat file.
Word Map on EC 1.15.1.2
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1.15.1.2
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desulfovibrio
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non-heme
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gigas
-
desulfoarculus
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baarsii
-
sulfate-reducing
-
high-spin
-
radiolysis
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rubrerythrin
-
hildenborough
-
hydroperoxo
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peroxo
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square-pyramidal
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ferric-hydroperoxo
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thiolate-ligated
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rubredoxin-like
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feiii-ooh
-
agriculture
- 1.15.1.2
- desulfovibrio
-
non-heme
- gigas
- desulfoarculus
- baarsii
-
sulfate-reducing
-
high-spin
-
radiolysis
- rubrerythrin
- hildenborough
-
hydroperoxo
-
peroxo
-
square-pyramidal
-
ferric-hydroperoxo
-
thiolate-ligated
-
rubredoxin-like
-
feiii-ooh
- agriculture
Reaction
Synonyms
1Fe SOR, 1Fe-SOR, 1Fe-superoxide reductase, 2Fe-SOR, class I SOR, class I superoxide reductase, class II SOR, cytochrome c–superoxide oxidoreductase, desulfoferrodoxin, desulforedoxin, Dfx, EC 1.18.96.1, Fe-SOR, GiSOR, MM_0632, More, neelaredoxin, neelaredoxin-type SOR, Nlr, PfSOR, rubredoxin oxidoreductase, SOR, superoxide reductase, TM0658, two-iron superoxide reductase, Zn/Fe-SOR
ECTree
1.15.1.2 superoxide reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.15.1.2 - superoxide reductase
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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
reduced acceptor + superoxide
acceptor + H2O2 + O2
-
enzyme is able to both reduce and dismutate superoxide
-
?
reduced acceptor + superoxide + H+
acceptor + H2O2
-
enzyme can be fully reduced upon addition of NADH or NADPH under anaerobic conditions
-
?
reduced cytochrome c + superoxide + 2 H+
oxidized cytochrome c + H2O2
oxygen cannot function as an electron acceptor
-
-
?
reduced cytochrome c + superoxide + 2 H+
oxidized cytochrome c + H2O2
oxygen cannot function as an electron acceptor
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
enzyme shows only very weak superoxide dismutase activity
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
enzyme shows only very weak superoxide dismutase activity
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
-
-
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
-
-
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
oxidized rubredoxin + H2O2
reduced rubredoxin from Clostridium acetobutylicum
-
-
?
reduced rubredoxin + superoxide + 2 H+
oxidized rubredoxin + H2O2
reduced rubredoxin from Clostridium acetobutylicum
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination, the reaction procedes via a Fe3+-peroxo intermediate
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
the mononuclear iron center with an FeN4S1 coordination catalyzes the one electron reduction of superoxide to form hydrogen peroxide in presence of an additional rubredoxin-like desulforedoxin iron center
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the enzyme may contribute to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the enzyme may contribute to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
superoxide reductase mediates reduction of superoxide to hydrogen peroxide in an NADPH-dependent manner via a coupled reaction between NAD(P)H:rubredoxin oxidoreductase, rubredoxin, and superoxide reductase
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
with NADH
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
with NADH
-
-
?
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
-
?
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
blue non-heme iron enzyme that functions in anaerobic microbes as a defense mechanism against reactive oxygen species by catalyzing the reduction of superoxide to H2O2
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
2 type I rubredoxins
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
SORs are nonheme iron-containing enzymes that remove superoxide by reducing it to hydrogen peroxide
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
desulfoferrodoxin functions as a superoxide reductase
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
functionally important residues are Glu47, Lys48, His49, His69, His75, His119, Ile77, and Cys116, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
functionally important residues are Glu46, Lys47, His48, His68, His74, His118, Ile76, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
functionally important residues are Glu47, Lys48, His49, His69, His75, His119, Ile77, and Cys116, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
probably via a ferric-hydroperoxo intermediate, which decays smoothly to the resting ferric active site with no other detectable intermediates, solvent proton donation occurs in the rate-determining step of dead time intermediate decay and neither of the conserved pocket residues, Glu47 or Lys48, functions as a rate-determining proton donor between pH 6.0 and pH 8.0
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
superoxide scavenging by superoxide reductases constitutes an alternative detoxifying system to the canonical superoxide dismutases, instead of dismutating superoxide, SORs catalyse only the reductive reaction, forming hydrogen peroxide as a product
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
functionally important residues are Glu14, Lys15, His16, His41, His51, His118, Ile49, and Cys111, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
SOR is a non-heme iron enzyme that reduces superoxide to peroxide at a diffusion-controlled rate, thiolate acts as a covalent anionic ligand. Replacing the thiolate with a neutral noncovalent ligand makes protonation very endothermic and greatly raises the reduction potential,overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
functionally important residues are Glu15, Lys16, His17, His45, His51, His118, Ile53, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
functionally important residues are Glu48, Lys49, His50, His70, His76, His122, Ile78, and Cys119, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
-
-
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
-
-
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
-
enzyme has O2 radical detoxification activity, catalyzed by the SOR-ferrocyanide complex, which does not conduct to the production of the toxic H2O2 species
-
-
?
additional information
?
-
a cysteinate sulfur bound to the iron site, as well as the positioning of the metal ion on the surface versus the interior of the protein, alters the function of Fe-superoxide reductase relative to Fe-superoxide dimutase
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-
?
additional information
?
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
in contrast to superoxide dismutases, EC 1.15.1.1, SORs do not catalyze the dismutation reaction of superoxide, but catalyze a one-electron reduction of superoxide to produce H2O2, without formation of O2, electron transfer mechanisms, detailed overview
-
-
?
additional information
?
-
-
artificial reduction of the SOR iron active site using the NADPH:flavodoxin oxidoreductase from Escherichia coli
-
-
?
additional information
?
-
-
photochemical properties of the SOR reaction intermediates, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
-
in times of oxidative stress, enzyme efficiently diverts intracellular reducing equivalents to superoxide
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
-
structure-function relationship, overview
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
nitric oxide is used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus superoxide reductase through the use of EPR, resonance Raman, Fourier transform IR, UV-visible absorption, and variabletemperature variable-field magnetic CD spectroscopies
-
-
?
additional information
?
-
-
nitric oxide is used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus superoxide reductase through the use of EPR, resonance Raman, Fourier transform IR, UV-visible absorption, and variabletemperature variable-field magnetic CD spectroscopies
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
Treponema palladium
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, overview
-
-
?
