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
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desulfoarculus
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baarsii
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sulfate-reducing
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high-spin
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radiolysis
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rubrerythrin
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hildenborough
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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
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agriculture
- 1.15.1.2
- desulfovibrio
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non-heme
- gigas
- desulfoarculus
- baarsii
-
sulfate-reducing
-
high-spin
-
radiolysis
- rubrerythrin
- hildenborough
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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
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 (Engineering
Engineering on EC 1.15.1.2 - superoxide reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E12Q
E12V
C13S
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site-directed mutagenesis, the lack of iron center I in the C13S SOR mutant does not significantly affect the folding of iron center II and its reactivity with superoxide
E114A
E47A
I118S
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site-directed mutagenesis, the mutat shows an altered active site compared to the wild-type and formation of a high-valent iron-oxo species when the mutant protein is reacted with H2O2.. For I118S, formation of the iron-oxo species can also result from the cleavage of the O-O bond of an FeIII-OOH intermediate
K48I
Y115A
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site-directed mutagenesis, the Y115A SOR mutant folds properly, this mutation does not affect the general properties of the two iron sites of SOR
E114A
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site-directed mutagenesis, crystal structure determination
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E46A
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site-directed mutagenesis, crystal structure determination
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E47A
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site-directed mutagenesis, crystal structure determination
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I118S
Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
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site-directed mutagenesis, the mutat shows an altered active site compared to the wild-type and formation of a high-valent iron-oxo species when the mutant protein is reacted with H2O2.. For I118S, formation of the iron-oxo species can also result from the cleavage of the O-O bond of an FeIII-OOH intermediate
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K48I
Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
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site-directed mutagenesis, the mutat shows an altered active site compared to the wild-type and formation of a high-valent iron-oxo species when the mutant protein is reacted with H2O2. For the K48I mutant, the Fe=O species is formed from the FeIII-OOH species
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C13S
E47A
K48A
P8E
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site-directed mutagenesis, pH-induced transition of the mutant is similar to the wild-type enzyme, the reactivity of the N. equitans P8E Nlr mutant towards superoxide measured at different pHs is identical to that of the wild-type protein
additional information
E12Q
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mutation in corrdination site of iron. Detailed kinetic analysis
E12Q
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lacking the highly conserved glutamate residue of the active site without profound influence on the iron binding behaviour
E12V
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mutation in corrdination site of iron. Detailed kinetic analysis
E12V
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lacking the highly conserved glutamate residue of the active site without profound influence on the iron binding behaviour
E12V
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redox properties of the mutant compared to the wild-type enzyme
E114A
site-directed mutagenesis, crystal structure determination
E114A
the mutant shows significantly modified pulse radiolysis kinetics for the protonation process of the first reaction intermediate compared to the wild-type enzyme, mutation results in both a strengthening of the S-Fe bond and an increase in the extent of freeze-trapping of a Fe-peroxo species after treatment with H2O2 by a specific strengthening of the Fe-O bond, spectroscopic mutant analysis, overview
E47A
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active site of the mutant can transiently stabilize an Fe3+ peroxo species
E47A
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E47 is not the base responsible for pH transitions, and not involved in formation of the first reaction intermediate
E47A
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FITR study, presence of E47 is important for the structural reorganization accompanying iron oxidation
E47A
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the electronic absorption band corresponding to the oxidized active site exhibits a pH-dependent alkaline transition changing from ca. 644 to 560 nm as the pH increases and with an apparent pKa of 9.0 in wild-type. In mutant E47A, this pKa shifts to 6.7
K48I
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20-fold lower second-order rate constant for the oxidation of the iron center by superoxide compared to wild-type enzyme, K48 may play a role in directing and stabilizing superoxide to the active site at center II
K48I
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FITR study, catalytic role of K48 is purely electrostatic, guiding superoxide toward the reduced iron
K48I
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K48 is not the base responsible for pH transitions, and not involved in formation of the first reaction intermediate
K48I
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the electronic absorption band corresponding to the oxidized active site exhibits a pH-dependent alkaline transition changing from ca. 644 to 560 nm as the pH increases and with an apparent pKa of 9.0 in wild-type. In mutant K48I, this pKa shifts to 7.6
K48I
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site-directed mutagenesis, the mutat shows an altered active site compared to the wild-type and formation of a high-valent iron-oxo species when the mutant protein is reacted with H2O2. For the K48I mutant, the Fe=O species is formed from the FeIII-OOH species
C13S
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destruction of native Fe(SCys)4 site with complete loss of its iron, no enzymic activity. Fe(NHis)4(SCys) site and protein homodimer remain intact
E47A
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E47 may interact with the iron atom of ferric center II, most likely by carboxylate ligation
E47A
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the mutation of 2Fe-SOR results in an identical 600 nm intermediate that decays at the same rate as for the wild-type protein at and above neutral pH, but to a solvent- rather than glutamate-ligated resting ferric SOR site, mutant enzyme kinetics in comparison to the wild-type enzyme
E47A
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redox properties of the mutant compared to the wild-type enzyme
K48A
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lysyl side chain may participate in directing the superoxide toward the active site and in directing the protonation pathway of the ferric-(hydro)peroxo intermediate toward release of hydrogen peroxide
K48A
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redox properties of the mutant compared to the wild-type enzyme
additional information
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the mutant enzymes lacking the glutamate and lysine residues close to the active site can be a competent superoxide reductase
additional information
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expression in Nicotiana tabacum as fusion protein with green fluorescent protein. Enzyme construct localizes to cytosol and nucleus. Enzyme retains its function and heat stability. Plant cells expressing the enzyme show enhanced survival at high temperatures
additional information
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construction of inactive 1754M strain containing the insertionally inactivated Td SOR gene
additional information
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construction of inactive 1754M strain containing the insertionally inactivated Td SOR gene
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