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
-
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
- 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
results (
results (Metals Ions
Metals Ions on EC 1.15.1.2 - superoxide reductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
-
at the dimer interface coordinated by eight oxygen atoms, Ser87, Thr89 from both monomers, and two water molecules
Fe
Fe2+
Fe2+/Fe3+
Iron
Zn2+
additional information
Fe
-
2Fe-SOR contains iron center I and iron center II, function of iron center I as an electronic relay between a reductase enzyme and iron center II, overview. The active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one electron reduction of superoxide to form hydrogen peroxide. Presence of an additional rubredoxin-like desulforedoxin iron center, which functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction
Fe
-
the enzyme contains a catalytic nonheme iron centre coordinated by four histidine ligands and one cysteine ligand
Fe2+
a nonheme iron-containing enzyme, 2Fe-SOR or desulfoferrodoxin class of superoxide reductases
Fe2+
the class I enzyme contains two iron-centers, while the class II enzyme contains one iron-center, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H14, H40, H46, C110, and H113. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
a non-heme iron enzyme, isolation of coordinatively unsaturated, mononuclear five coordinate thiolate iron complexes, including [FeIII-(S2Me2N3(Pr,Pr))]+, [FeIII(S2Me2N3-(Et,Pr))]+, and [FeII(SMe2N4(tren))]+
Fe2+
a non-heme, iron-containing enzyme, in the catalytically active reduced state, SORs contain a high-spin FeII center ligated by four equatorial histidine units and one apical cysteinate residue trans to an open site. Additionally, a number of SORs also contain a second rubredoxin-like [Fe(SCys)4] center, complex formation, kinetics, and electrochemistry, overview
Fe2+
the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination
Fe2+
the class I enzyme contains two iron-centers, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
-
SOR is a small non-heme mononuclear iron protein, formation of high-valent iron-oxo species in superoxide reductase, analysis by resonance Raman spectroscopy, overview
Fe2+
-
complex formation, kinetics, and electrochemistry, overview
Fe2+
-
the class I enzyme contains two iron-centers, i.e. two iron atoms per subunit, binding structure, overview
Fe2+
-
catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
the class I enzyme contains two iron-centers, binding structure, overview
Fe2+
-
catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
-
catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
-
one Fe per monomer, consistent with full occupancy of the metal center in the active site of the enzyme
Fe2+
a 1Fe-SOR, the iron centre is highly sensitive to photoreduction. The N-terminal loop of the protein, containing the characteristic EKHxP motif, reveals an unusually high flexibility regardless of the iron redox state. Each GiSOR monomer displays a solvent-exposed active site containing one Fe atom. The high solvent accessibility of the metal has been proposed to be important for the catalytic function of the enzyme, as it ensures easy access of superoxide anion to the active site and its prompt reduction to hydrogen peroxide. The Fe atom displays octahedral coordination geometry and is coordinated by residues located in loops connecting beta-strands: the imidazole rings of His19, His40, His46 and His102 in the equatorial plane, with the Cys99 S atom and one carboxylate O atom from Glu17 occupying the two axial positions
Fe2+
a non-heme iron enzyme, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112, metal binding site structure, overview
Fe2+
catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
Megalodesulfovibrio gigas
-
the class II enzyme contains one iron-center, binding structure, overview
Fe2+
Megalodesulfovibrio gigas
-
the class II enzyme has a single redox catalytic center consisting of an Fe atom bound to four nitrogen atoms from histidine side chains in the equatorial plane and to one cysteine sulfur in the axial plane
Fe2+
-
the class I enzyme contains two iron-centers, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H10, H35, H41, C97, and H100. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
1Fe SOR is a non-heme iron enzyme, iron binding and reaction mechanism, detailed overview
Fe2+
the class II enzyme contains one iron-center, iron ligands Glu14, His47 and His114 in addition to adjacent residues Trp11, Ile39, Pro40, Pro42, Thr44 and Ile113, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
catalytic Fe2+ binding residues are H25, H50, H56, C111, and H114. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
the class II enzyme contains one iron-center, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+
-
the class III enzyme contains one iron-center, a homodimer containing a sole iron site per monomer, binding structure, overview
Fe2+
catalytic Fe2+ binding residues are H50, H70, H76, C119, and H122. With the exception of the class IV (methanoferrodoxins) and the atypical SORs, they all appear to contain one or two iron centers: the catalytic center plus the desulforedoxin-like and rubredoxin-like, Dx/Rb-like, center
Fe2+/Fe3+
-
1.97 iron atoms/subunit, enzyme contains two Fe-centers: center I contains a mononuclear ferric iron coordinated by four cysteines in distorted rubredoxin-type center, center II has a ferrous iron with square pyramidal coordination to four nitrogens from histidines as equatorial ligands and one sulfur from a cysteine as the axial ligand, the reduced form of center II can transfer 1 electron to superoxid anion very efficiently
Fe2+/Fe3+
-
in the oxidized state, the mononuclear ferric active site has a octahedral coordination with four equatorial histidyl ligands and axial cysteinate and monodentate glutamate ligands, in the reduced state the ferrous site has a square-pyramidal coordination geometry in frozen solution with four equatorial histidines and one axial cysteine
Fe2+/Fe3+
each subunit contains a single mononuclear non-heme iron center
Fe2+/Fe3+
-
0.67 iron atoms/subunit, iron atom exists as a mononuclear center in a mixture of high spin ferrous and ferric oxidation states
Iron
-
0.8 atoms per subunit for wild-type, mutant E12V, 1.2 atoms per subunit, mutant E12Q, 0.9 atoms per subunit
Iron
-
1Fe-SOR and 2Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
-
EPR analysis of wild-type and mutant E48A. Rapid treatment with H2O2 results in the stabilization of a side-on high spin Fe3+-(eta2-OO) peroxo species. Comparison between Treponema pallidum and Desulfoarctus baarsii enzyme
Iron
-
investigation on reactivity of the SOR–ferrocyanide complex with O2 radical by pulse and gamma-ray radiolysis, infrared, and UV-visible spectroscopies. A one-electron redox chemistry is carried out by the ferrocyanide moiety of the complex, whereas the SOR iron site remains in the reduced state. The toxic H2O2 species is no longer the reaction product
Iron
-
non-heme iron in square-pyramidal [His4Cys] coordination. At basic pH a high-spin Fe3+-OH species is formed at the active site, which upon protonation results in a water molecule in the active site
Iron
-
2Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
2Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
-
an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
-
the redox-linked changes of the enzyme, as monitored by IR difference spectroscopy, indicate the reversible dissociation of glutamate E23 from the active site iron upon reductive activation, thereby enabling substrate binding and transformation
Iron
Megalodesulfovibrio gigas
-
an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
the enzyme contains a [Fe(NHis)4(SCys)] site as the catalytic center and an [4Fe–4S] cluster as second prosthetic group that is probably involved in electron transfer to the catalytic center
Iron
-
an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant. The electrostatic surface close to center II has a positive character, mainly due to the metal ion and to residue Lys 15 of 1Fe-SOR, metal site structure and mechanism, overview
Iron
-
resonance Raman characterization of the mononuclear iron active-site
Iron
1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
Iron
-
EPR analysis of wild-type and mutant E48A. Rapid treatment with H2O2 results in the stabilization of a side-on high spin Fe3+-(eta2-OO) peroxo species. Comparison between Treponema pallidum and Desulfoarctus baarsii enzyme. Above pH 8.5, the iron centre of Treponema pallidum becomes unstable and no spectra can be obtained
Iron
-
1Fe-SOR, an iron ion is bound at the catalytic site to four histidines and a cysteine that, in its reduced form, reacts with superoxide anion with a diffusion-limited second order rate constant, metal site structure and mechanism, overview
additional information
binding of synthetic iron ligand complexes, overview
additional information
-
binding of synthetic iron ligand complexes, overview
additional information
-
metal content and protein quantification, overview
additional information
-
SORs can be classified as 1Fe-SORs, or neelaredoxins, or as 2Fe-SORs, or desulfoferrodoxins, according to the number of metal centres
additional information
Megalodesulfovibrio gigas
-
ionic strength dependence of superoxide-mediated rubredoxin oxidation
additional information
binding of synthetic iron ligand complexes, overview
additional information
-
no other metal-binding domain besides the non-heme [Fe(His)4Cys] sites
additional information
Treponema palladium
-
binding of synthetic iron ligand complexes, overview
