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Information on EC 1.15.1.2 - superoxide reductase and Organism(s) Pyrococcus furiosus and UniProt Accession P82385
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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: Pyrococcus furiosus
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, neelaredoxin-type sor, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
desulforedoxin
-
-
-
-
SOR
additional information
the enzyme belongs to the class II of superoxide reductases
SOR
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
reaction mechanism of SOR involving transfer of an electron and two protons to superoxide to form hydrogen peroxide, kinetic mechanism, detailed overview
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, geometry of the catalytic center, oxidative cycle/reductive pathway, overview
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
catalytic mechanism with the first step involving oxidative addition of superoxide to form a ferric-peroxo intermediate. The Fe spin state and the trans cysteinate ligand play an important role in effecting superoxide reduction and peroxide release
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
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-
-
-
reduction
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-
-
-
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 + 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
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
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-
-
?
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
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
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-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
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-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
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-
-
?
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 + H+
rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
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?
additional information
?
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
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-
?
additional information
?
-
structure-function relationship, overview
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-
?
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
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-
?
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
-
-
?
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
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
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
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 + H+
oxidized rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
structure of the neelaredoxin center, oxidized and reduced forms, overview
-
reduced rubredoxin
a potential Rd binding site is located in the vicinity of the solvent-exposed residues that are close to the iron centre
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+/Fe3+
each subunit contains a single mononuclear non-heme iron center
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
Fe2+/Fe3+
Iron
-
resonance Raman characterization of the mononuclear iron active-site
additional information
binding of synthetic iron ligand complexes, overview
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+/Fe3+
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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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic analysis, binding parameters, and electrochemic parameters of the enzyme and Fe2+ complexes, overview
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additional information
additional information
-
kinetic analysis, binding parameters, and electrochemic parameters of the enzyme and Fe2+ complexes, overview
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
enzyme functions efficiently in vitro at 25°C, which is 75°C below the organism's optimal growth temperature
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
recombinant enzyme within midgut proteins extracted from transgenic Bombyx mori strain A4SOR and nontransgenic strain Dazao larvae on day 3 of the fifth instar
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
physiological function
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
-
enzyme SOR efficiently detoxifies reactive oxygen species. Overexpression of SOD can improve the tolerance of transgenic organisms to various oxidative stresses
additional information
additional information
activity remains essentially unchanged with change in the growth condition (maltose + peptides, maltose, maltose + peptides + sulfur S(0), maltose + sulfur S(0), peptides + sulfur S(0))
additional information
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
additional information
primary structure, structure-function relationship, overview
additional information
three-dimensional structure of the neelaredoxin, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of the reduced or the oxidized and Glu bound wild-type enzyme, PDB IDs 1DQI, 1DO6, and 1DQK
crystal structure determination at 2.0 A and 1.7 A resolution, respectively, PDB IDs 1DO6 and 1DQI
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the enzyme can be produced as a functional enzyme in planta and that plants producing SOR have enhanced tolerance to heat, light, and chemically induced reactive oxygen species
PfSOR, synthesis of an artificial DNA sequence (referred to as SOR-as) based on the PfSOR gene sequence No AE010234 and on codon bias of Bombyx mori and expression as FLAG-tagged enzyme in transgenic Bombyx mori strain A4SOR and in Bombyx mori BmE cells, the A4SOR insertion occurs on chromosome 10 in an intergenic region separated from the nearest genes to the left and right by 22 and 47 kb, respectively, Non-diapausing DZ embryos are microinjected with pb-A4SOR. Construction of vector 1180-hr3-A4P-Flag-SOR-His-SV4 and functionalrecombinant overexpression of C-terminally His-tagged enzyme, RT-PCR enzyme expression analysis and patterns in recombinant cells and transgenic in 8-day-old eggs, hatched silkworms, first instar molts, second instar larvae, second instar molts, third instar larvae, third instar molts, fourth instar larvae, fourth instar molts, fifth instar larvae, wandering silkworm, and pupae, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity remains essentially unchanged with change in the growth condition (maltose + peptides, maltose, maltose + peptides + sulfur S(0), maltose + sulfur S(0), peptides + sulfur S(0))
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jenney, F.E., Jr.; Verhagen, M.F.J.M.; Cui, X.; Adams, M.W.W.
Anaerobic microbes: oxygen detoxification without superoxide dismutase
Science
286
306-309
1999
Pyrococcus furiosus
Yeh, A.P.; Hu, Y.; Jenney, F.E., Jr.; Adams, M.W.W.; Rees, D.C.
Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states
Biochemistry
39
2499-2508
2000
Pyrococcus furiosus (P82385), Pyrococcus furiosus
Clay, M.D.; Jenney, F.E., Jr.; Hagedoorn, P.L.; George, G.N.; Adams, M.W.W.; Johnson, M.K.
Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism
J. Am. Chem. Soc.
124
788-805
2002
Pyrococcus furiosus
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
Im, Y.J.; Ji, M.; Lee, A.M.; Boss, W.F.; Grunden, A.M.
Production of a thermostable archaeal superoxide reductase in plant cells
FEBS Lett.
579
5521-5526
2005
Pyrococcus furiosus
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)
-
Dey, A.; Jenney, F.E.; Adams, M.W.; Johnson, M.K.; Hodgson, K.O.; Hedman, B.; Solomon, E.I.
Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on superoxide reductase: role of the axial thiolate in reactivity
J. Am. Chem. Soc.
129
12418-12431
2007
Pyrococcus furiosus (P82385), Pyrococcus furiosus
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
Grunden, A.M.; Jenney, F.E.; Ma, K.; Ji, M.; Weinberg, M.V.; Adams, M.W.
In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus
Appl. Environ. Microbiol.
71
1522-1530
2005
Pyrococcus furiosus
Clay, M.D.; Jenney, F.E.; Noh, H.J.; Hagedoorn, P.L.; Adams, M.W.; Johnson, M.K.
Resonance Raman characterization of the mononuclear iron active-site vibrations and putative electron transport pathways in Pyrococcus furiosus superoxide reductase
Biochemistry
41
9833-9841
2002
Pyrococcus furiosus
Im, Y.J.; Ji, M.; Lee, A.; Killens, R.; Grunden, A.M.; Boss, W.F.
Expression of Pyrococcus furiosus superoxide reductase in Arabidopsis enhances heat tolerance
Plant Physiol.
151
893-904
2009
Pyrococcus furiosus (P82385), Pyrococcus furiosus
Clay, M.D.; Cosper, C.A.; Jenney, F.E.; Adams, M.W.; Johnson, M.K.
Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase
Proc. Natl. Acad. Sci. USA
100
3796-3801
2003
Pyrococcus furiosus (P82385), Pyrococcus furiosus
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)
Jiang, L.; Huang, C.; Wang, B.; Guo, H.; Sun, Q.; Xia, F.; Xu, G.; Xia, Q.
Enhanced heat tolerance in transgenic silkworm via overexpression of Pyrococcus furiosus superoxide reductase
Insect Biochem. Mol. Biol.
92
40-44
2017
Pyrococcus furiosus
Adams, M.; Holden, J.; Menon, A.; Schut, G.; Grunden, A.; Hou, C.; Hutchins, A.; Jenney F.E., J.; Kim, C.; Ma, K.; Pan, G.; Roy, R.; Sapra, R.; Story, S.; Verhagen, M.
Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
716-724
2001
Pyrococcus furiosus (P82385)
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