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
Advanced search results
Cofactor
Cofactor 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.
Megalodesulfovibrio gigas
-
endogenous, contains Zn2+, the protein is able to transfer electrons to superoxide reductase with a maximum kapp of 31/min at an ionic strength of 57 mM, the enzyme complex with superoxide reductase is not detected by chemical shift perturbation
reduced rubredoxin
a potential Rd binding site is located in the vicinity of the solvent-exposed residues that are close to the iron centre
-
reduced rubredoxin
rubredoxin is reduced by ferredoxin:NADP+ reductase from spinach and NADPH
-
rubredoxin
-
contains on-heme [Fe(His)4Cys] active sites. Enzymatic reduction of the enzyme iron sites with use of NADH:rubredoxin oxidoreductase and rubredoxin, both from Thermotoga maritima, rates of enzymatic reduction of the ferric center I and enzyme sites are measured
-
rubredoxin
Megalodesulfovibrio gigas
-
endogenous. A monomeric, non-heme iron protein that contains a tetrahedral FeS4 metal center. The rubredoxin surface involved in the electron transfer complex with superoxide reductase comprises the solvent-exposed hydrophobic residues in the vicinity of its metal center, Cys9, Gly10, Cys42, Gly43, and Ala44. Kd of 0.003 mM at 59 mM ionic strength by NMR. Model structure of superoxide reductase-rubredoxin complex, overview
-
rubredoxin
-
rubredoxins, small proteins with a [FeCys4] center known to be involved in electron transfer processes, are generally assumed to be the direct electron donors to SOR, based on the fact that the genes encoding rubredoxin and SOR lie in the same operon in some bacteria. Consistently, reduced rubredoxins are shown to reduce both 1Fe- and 2Fe-SORs, but physiological electron donors other than rubredoxins must exist because rubredoxins are missing in a large number of organisms that encode SORs
-
structure of the neelaredoxin center, oxidized and reduced forms, overview
-
additional information
-
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, that functions as an electronic relay between cellular reductases and the iron active site for superoxide reduction
-
additional information
-
the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview
-
additional information
Megalodesulfovibrio gigas
-
the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview
-
additional information
the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview
-
additional information
Megalodesulfovibrio gigas
-
titration of Zn-rubredoxin with superoxide reductase, overview. NMR competition assay between desulforedoxin and rubredoxin for binding to SOR, overview
-