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Information on EC 1.15.1.2 - superoxide reductase and Organism(s) Desulfarculus baarsii and UniProt Accession Q46495
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1.15.1.2 superoxide reductaseIUBMB Comments
The enzyme contains non-heme iron.
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Word Map
- 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
The taxonomic range for the selected organisms is: Desulfarculus baarsii
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
reduced rubredoxin
+
2
=
+
oxidized rubredoxin
Synonyms
superoxide reductase, neelaredoxin, desulfoferrodoxin, desulforedoxin, rubredoxin oxidoreductase, 2fe-sor, pfsor, 1fe-sor, two-iron superoxide reductase, gisor, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
desulforedoxin
-
-
-
-
SOR
additional information
the enzyme belongs to the class I of superoxide reductases
SOR
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
the iron in the actice site is coordinated through a bent cyano bridge, photo-reduction from FeIII to FeII induces an expansion of the enzyme active site
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
enzyme active site structure and mechanism
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
enzyme active site structure and mechanism, catalytic cycle involving iron complexes, overview
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
enzyme active site structure and mechanism, proposed mechanism for SOR-catalyzed reduction of superoxide via hydroperoxo and solvent-bound intermediates, catalytic cycle involving iron complexes, overview
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
very fast bimolecular reaction of iron center II with superoxide, followed by the formation of two successive intermediate species
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reduction of superoxide may proceed through Fe3+-peroxo intermediates
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
FITR study, presence of E47 is important for the structural reorganization accompanying iron oxidation, catalytic role of K48 is purely electrostatic, guiding superoxide toward the reduced iron
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
in absence of O2.-, reduction potential and absorption spectrum of the iron center II exhibit a pH transition. First reaction intermediate is an iron(III)-peroxo species, second intermediate is an iron(III)-hydroperoxo species
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism of the SOR with superoxide, overview
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
rubredoxin:superoxide oxidoreductase
The enzyme contains non-heme iron.
CAS REGISTRY NUMBER
COMMENTARY
250679-67-5
-
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 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
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
enzyme shows only very weak superoxide dismutase activity
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
-
-
-
-
?
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 + 2 H+
rubredoxin + H2O2
-
-
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
structure-function relationship, 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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
-
-
-
-
?
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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
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
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+/Fe3+
Iron
additional information
binding of synthetic iron ligand complexes, overview
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+/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
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 SORferrocyanide 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics, resonance Raman spectroscopy
-
additional information
additional information
-
kinetics, resonance Raman spectroscopy
-
additional information
additional information
-
kinetic analysis, e.g. kinetics of the formation of the first reaction intermediate T1 adjusted with a biexponential model, overview
-
additional information
additional information
-
stopped-flow kinetic analysis, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Fe-SOR classification, detailed overview. One classification takes into consideration the primary and tertiary structures of SORs some enzymes contain only one Fe ion, but have a longer N-terminus with amino acid sequence and structural similarities with those of the respective domain of desulfoferrodoxins, but lacking the cysteine ligands to the desulforedoxin (Dfxs)-like center. According to the authors, SORs fall into three classes: classes I (Dfxs), II (neelaredoxins), and III (neelaredoxins structurally homologous to desulfoferrodoxins, with only one Fe center). In dendograms constructed from available amino acid sequences, class III enzymes cluster within the class I enzymes, it is plausible that class III SORs evolved from class I proteins by loss of the cysteine residues binding the desulforedoxin-like center, an event that may have occurred more than once because the Dfxs are not monophyletic. This classification misses the family of methanoferrodoxins. Another classification is based on the variability of N-terminal domains classifying SORs into seven classes. Class I or Dx-SOR includes the 2Fe-SORs, where the N-terminal is a desulforedoxin-like (Dx) domain. Class II includes the 1Fe-SORs that have no extra N-terminal domain. Class III SORs are analogous to Dx-SORs but lacking some or all of the Fe cysteine ligands (FeCys4) for the desulforedoxin-like Fe center and therefore lacking the FeCy4 site. Class IV includes SORs with an extra C-terminal domain containing an iron-sulfur center. The fifth class, termed HTH-Dx-SOR, includes Dx-SORs (2Fe-SOR) with an extended N-terminal helix-turn-helix domain present in transcription regulators. The sixth class, termed TAT-SOR, includes SORs from only a few organisms and the sequences are preceded by a putative twin-arginine signal peptide that suggests their periplasmic localization
malfunction
-
mutation of two residues in the second coordination sphere of the SOR iron active site, K48 and I118, leads to the formation of a high-valent iron-oxo species when the mutant proteins are reacted with H2O2
physiological function
additional information
physiological function
-
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
-
superoxide reductase is involved in superoxide detoxification
physiological function
-
superoxide reductase, SOR, is a superoxide detoxification system, with a role of the rubredoxin-like iron center in the superoxide detoxifying activity of SOR, overview
physiological function
-
superoxide reductase (SOR )is a small non-heme iron protein that is not involved in oxidation reactions, but in superoxide radical detoxification in microorganisms
additional information
key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118
additional information
-
the SOR active site is located at the surface of the protein and consists of a mononuclear iron center, named center II, pentacoordinated in its ferrous state by four nitrogen atoms from histidine residues in an equatorial plane and one sulfur atom from a cysteine residue in an axial position. It displays a high redox potential. 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
additional information
-
the enzyme is used as an unprecedented model to study the mechanisms of O2 activation and of the formation of high-valent iron-oxo species in metalloenzymes. Formation of high-valent iron-oxo species in superoxide reductase, analysis by resonance Raman spectroscopy, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
structure-function relationship, overview
homodimer
-
three-dimensional structure of the homodimeric SOR, modelling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures determination of wild/tzp and mutant enzymes at 1.15-1.95 A resolution, PDB IDs 1VZI, 1VZG, 1VZH, 2JI1, 2JI2, and 2JI3
mutant E47A, alone and in complex with ferrocyanide, the iron in the actice site is coordinated through a bent cyano bridge
crystal structure analysis of the wild-type and E114A mutant enzymes in different oxidation states, PDB IDs 2JI3, 2JI2, 2JI1, and 1VZI
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E114A
E47A
C13S
-
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
E47A
I118S
-
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
-
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
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
-
active site of the mutant can transiently stabilize an Fe3+ peroxo species
E47A
-
E47 is not the base responsible for pH transitions, and not involved in formation of the first reaction intermediate
E47A
-
FITR study, presence of E47 is important for the structural reorganization accompanying iron oxidation
E47A
-
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
-
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
-
FITR study, catalytic role of K48 is purely electrostatic, guiding superoxide toward the reduced iron
K48I
-
K48 is not the base responsible for pH transitions, and not involved in formation of the first reaction intermediate
K48I
-
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant SORs, and rubredoxin from Escherichia coli strain BL21(DE3) to homogeneity by anion exchange chromatography and gel filtration
-
so far there is no suitable enzymatic assay for monitoring the purification from cell extracts
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene sor, complementation of the Escherichia coli QC2375 mutant strain
expression of wild-type and mutant SORs, and of rubredoxin in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lombard, M.; Fontecave, M.; Touati, D.; Niviere, V.
Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity
J. Biol. Chem.
275
115-121
2000
Desulfarculus baarsii
Lombard, M.; Houee-Levin, C.; Touati, D.; Fontecave, M.; Niviere, V.
Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis
Biochemistry
40
5032-5040
2001
Desulfarculus baarsii
Mathe, C.; Mattioli, T.A.; Horner, O.; Lombard, M.; Latour, J.M.; Fontecave, M.; Niviere, V.
Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii
J. Am. Chem. Soc.
124
4966-4967
2002
Desulfarculus baarsii
Rusnak, F.; Ascenso, C.; Moura, I.; Moura, J.J.G.
Superoxide reductase activities of neelaredoxin and desulfoferrodoxin metalloproteins
Methods Enzymol.
349
243-258
2002
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio vulgaris, Pyrococcus furiosus, Treponema pallidum
Niviere, V.; Lombard, M.
Superoxide reductase from Desulfoarculus baarsii
Methods Enzymol.
349
123-129
2002
Desulfarculus baarsii, Treponema pallidum
Berthomieu, C.; Dupeyrat, F.; Fontecave, M.; Vermeglio, A.; Niviere, V.
Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study
Biochemistry
41
10360-10368
2002
Desulfarculus baarsii
Niviere, V.; Asso, M.; Weill, C.O.; Lombard, M.; Guigliarelli, B.; Favaudon, V.; Houee-Levin, C.
Superoxide reductase from Desulfoarculus baarsii: identification of protonation steps in the enzymatic mechanism
Biochemistry
43
808-818
2004
Desulfarculus baarsii
Adam, V.; Royant, A.; Niviere, V.; Molina-Heredia, F.P.; Bourgeois, D.
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
Structure
12
1729-1740
2004
Desulfarculus baarsii (Q46495), Desulfarculus baarsii
Mathe, C.; Niviere, V.; Houee-Levin, C.; Mattioli, T.A.
Fe(3+)-eta(2)-peroxo species in superoxide reductase from Treponema pallidum. Comparison with Desulfoarculus baarsii
Biophys. Chem.
119
38-48
2006
Desulfarculus baarsii, Treponema pallidum
Mathe, C.; Niviere, V.; Mattioli, T.A.
Fe3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes
J. Am. Chem. Soc.
127
16436-16441
2005
Desulfarculus baarsii
Molina-Heredia, F.P.; Houee-Levin, C.; Berthomieu, C.; Touati, D.; Tremey, E.; Favaudon, V.; Adam, V.; Niviere, V.
Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide
Proc. Natl. Acad. Sci. USA
103
14750-14755
2006
Desulfarculus baarsii
Kovacs, J.A.; Brines, L.M.
Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase
Acc. Chem. Res.
40
501-509
2007
Desulfarculus baarsii (Q46495)
Pereira, A.S.; Tavares, P.; Folgosa, F.; Almeida, R.M.; Moura, I.; Moura, J.J.
Superoxide reductases
Eur. J. Inorg. Chem.
2007
2569-2581
2007
Archaeoglobus fulgidus (O29903), Desulfarculus baarsii (Q46495), Desulfovibrio desulfuricans, Desulfovibrio vulgaris (P20418), Megalodesulfovibrio gigas, Methanothermobacter thermautotrophicus, Pyrococcus furiosus (P82385), Thermotoga maritima (Q9WZC6), Treponema pallidum
-
Brines, L.M.; Kovacs, J.A.
Understanding the mechanism of superoxide reductase promoted reduction of superoxide
Eur. J. Inorg. Chem.
2007
29-38
2007
Desulfovibrio desulfuricans, Treponema palladium, Pyrococcus furiosus (P82385), Desulfarculus baarsii (Q46495)
-
Mathe, C.; Weill, C.O.; Mattioli, T.A.; Berthomieu, C.; Houee-Levin, C.; Tremey, E.; Niviere, V.
Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii
J. Biol. Chem.
282
22207-22216
2007
Desulfarculus baarsii (Q46495), Desulfarculus baarsii
Pinto, A.; Rodrigues, J.; Teixeira, M.
Reductive elimination of superoxide: Structure and mechanism of superoxide reductases
Biochim. Biophys. Acta
1804
285-297
2010
Archaeoglobus fulgidus, Desulfarculus baarsii, Desulfovibrio desulfuricans (P22076), Desulfovibrio vulgaris, Megalodesulfovibrio gigas, Nanoarchaeum equitans, Pyrococcus furiosus (P82385), Pyrococcus horikoshii (O58810), Pyrococcus horikoshii OT-3 (O58810), Thermotoga maritima (Q9WZC6), Treponema pallidum
Bonnot, F.; Houee-Levin, C.; Favaudon, V.; Niviere, V.
Photochemical processes observed during the reaction of superoxide reductase from Desulfoarculus baarsii with superoxide. Re-evaluation of the reaction mechanism
Biochim. Biophys. Acta
1804
762-767
2010
Desulfarculus baarsii
Bonnot, F.; Duval, S.; Lombard, M.; Valton, J.; Houee-Levin, C.; Niviere, V.
Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site
J. Biol. Inorg. Chem.
16
889-898
2011
Desulfarculus baarsii
Bonnot, F.; Tremey, E.; von Stetten, D.; Rat, S.; Duval, S.; Carpentier, P.; Clemancey, M.; Desbois, A.; Niviere, V.
Formation of high-valent iron-oxo species in superoxide reductase characterization by resonance Raman spectroscopy
Angew. Chem. Int. Ed. Engl.
53
5926-5930
2014
Desulfarculus baarsii, Desulfarculus baarsii ATCC 33931 / DSM 2075 / VKM B-1802 / 2st14
Sheng, Y.; Abreu, I.; Cabelli, D.; Maroney, M.; Miller, A.; Teixeira, M.; Valentine, J.
Superoxide dismutases and superoxide reductases
Chem. Rev.
114
3854-3918
2014
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O29903), Archaeoglobus fulgidus ATCC 49558 (O29903), Desulfarculus baarsii (Q46495), Desulfarculus baarsii ATCC 33931 (Q46495), Desulfovibrio desulfuricans, Desulfovibrio vulgaris, Dosidicus gigas, Ignicoccus hospitalis (A8AC72), Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 (A8AC72), Nanoarchaeum equitans (Q74MF3), Pyrococcus furiosus (P82385), Pyrococcus furiosus ATCC 43587 (P82385), Pyrococcus horikoshii (O58810), Thermotoga maritima (Q9WZC6), Thermotoga maritima ATCC 43589 (Q9WZC6), Treponema pallidum (O82795), Treponema pallidum Nichols (O82795)
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