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superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
-
-
-
-
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
presence of Fe(NHis)4(SCys) site is sufficient to catalyze reduction of the intracellular superoxide to nonlethal levels
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
steady state kinetics, diffusion-controlled reaction of reduced enzyme with superoxide is the slowest process during turnover, neither ligation nor deligation of the active site carboxylate limits turnover rate
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
stopped-flow kinetics of electron transfer, second-order rate constant of 10 million M-1 s-1 at 10°C and pH 7.2
-
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
the initial reaction between O2- and Archaeoglobus fulgidus neelaredoxin leads to a short-lived transient that immediately disappears to yield a solvent-bound ferric species in acid-base equilibrium. The final step corresponds to the slow binding of the glutamate sixth ligand to the oxidized iron, a process that may be bypassed during in vivo catalytic turnover of the enzyme
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
the initial reaction involves the formation of a short-lived transient that decays by a proton-dependent step. This process generates an Fe3+OH species, which is converted to a glutamate-bound one. The function of center I of Dfx remains to be elucidated. The completion of the catalytic cycle of SOR, which involves the re-reduction of the active site, can be attained by reduced rubredoxin
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
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
enzyme active site structure and mechanism
Megalodesulfovibrio gigas
-
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
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
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
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, catalytic cycle involving iron complexes, overview
Treponema palladium
-
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, 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
reaction mechanism involves the diffusion-limited encounter of superoxide with the reduced iron site and concomitant formation of an Fe3+-(hydro)peroxo adduct that, upon protonation, leads to the formation of hydrogen peroxide. By the end of this process, a glutamate residue coordinates the ferric ion, acting as a sixth ligand
-
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, the active center of SORs consists of a ferrous ion coordinated by four histidines and one cysteine in a square-pyramidal geometry, formation of a hydroxo-iron ligated species upon the decay of the first transient species followed by conversion to the final species upon binding of the glutamate sixth ligand, phosphate can serve as an exogenous sixth ligand, overview
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, geometry of the catalytic center, oxidative cycle/reductive pathway, 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
reaction mechanism, oxidative cycle/reductive pathway, overview
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
Megalodesulfovibrio gigas
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
-
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, 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
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin
reaction mechanism, oxidative cycle/reductive pathway, overview
-
-
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reduced acceptor + superoxide
acceptor + H2O2 + O2
-
enzyme is able to both reduce and dismutate superoxide
-
?
reduced acceptor + superoxide + H+
acceptor + H2O2
-
enzyme can be fully reduced upon addition of NADH or NADPH under anaerobic conditions
-
?
reduced cytochrome c + superoxide + 2 H+
oxidized cytochrome c + H2O2
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
reduced rubredoxin + superoxide + 2 H+
oxidized rubredoxin + H2O2
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
additional information
?
-
reduced cytochrome c + superoxide + 2 H+
oxidized cytochrome c + H2O2
oxygen cannot function as an electron acceptor
-
-
?
reduced cytochrome c + superoxide + 2 H+
oxidized cytochrome c + H2O2
oxygen cannot function as an electron acceptor
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
enzyme shows only very weak superoxide dismutase activity
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
-
-
?
reduced cytochrome c + superoxide + H+
cytochrome c + H2O2
-
enzyme shows only very weak superoxide dismutase activity
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
-
-
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
-
-
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
oxidized rubredoxin + H2O2
reduced rubredoxin from Clostridium acetobutylicum
-
-
?
reduced rubredoxin + superoxide + 2 H+
oxidized rubredoxin + H2O2
reduced rubredoxin from Clostridium acetobutylicum
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
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
-
-
?
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
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the enzyme may contribute to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the enzyme may contribute to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
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 + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
with NADH
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
with NADH
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
-
?
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
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
2 type I rubredoxins
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
SORs are nonheme iron-containing enzymes that remove superoxide by reducing it to hydrogen peroxide
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
desulfoferrodoxin functions as a superoxide reductase
-
-
?
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 + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
functionally important residues are Glu46, Lys47, His48, His68, His74, His118, Ile76, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
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 + H+
rubredoxin + H2O2
-
probably via a ferric-hydroperoxo intermediate, which decays smoothly to the resting ferric active site with no other detectable intermediates, solvent proton donation occurs in the rate-determining step of dead time intermediate decay and neither of the conserved pocket residues, Glu47 or Lys48, functions as a rate-determining proton donor between pH 6.0 and pH 8.0
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
superoxide scavenging by superoxide reductases constitutes an alternative detoxifying system to the canonical superoxide dismutases, instead of dismutating superoxide, SORs catalyse only the reductive reaction, forming hydrogen peroxide as a product
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
?
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
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
functionally important residues are Glu15, Lys16, His17, His45, His51, His118, Ile53, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
Treponema palladium
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
functionally important residues are Glu48, Lys49, His50, His70, His76, His122, Ile78, and Cys119, mechanistic aspects of biological superoxide anion reduction, overview
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
-
-
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
-
-
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, 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
?
-
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
?
-
-
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
-
-
?
additional information
?
-
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
-
in times of oxidative stress, enzyme efficiently diverts intracellular reducing equivalents to superoxide
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
-
structure-function relationship, overview
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, overview
-
-
?
additional information
?
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
structure-function relationship, overview
-
-
?
additional information
?
-
Treponema palladium
-
comparison of superoxide reductase with superoxide dismutase, biomimetic models of SOR, overview
-
-
?
additional information
?
-
-
structure-function relationship, overview
-
-
?
additional information
?
-
-
redox properties of SOR's catalytic center, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
additional information
?
-
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
-
-
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
-
-
-
-
?
reduced desulforedoxin + superoxide + 2 H+
desulforedoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the enzyme may contribute to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
the enzyme may contribute to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
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 + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + 2 H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
oxidized rubredoxin + H2O2
-
rubredoxin is assumed to be the physiological electron carrier
-
-
?
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
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium
-
-
?
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
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
Megalodesulfovibrio gigas
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
superoxide scavenging by superoxide reductases constitutes an alternative detoxifying system to the canonical superoxide dismutases, instead of dismutating superoxide, SORs catalyse only the reductive reaction, forming hydrogen peroxide as a product
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
Treponema palladium
-
-
-
-
?
reduced rubredoxin + superoxide + H+
rubredoxin + H2O2
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced acceptor + 2 H+
H2O2 + oxidized acceptor
-
-
-
?
superoxide + reduced rubredoxin + 2 H+
H2O2 + oxidized rubredoxin
-
-
-
-
?
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
-
-
?
additional information
?
-
-
in times of oxidative stress, enzyme efficiently diverts intracellular reducing equivalents to superoxide
-
-
?
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Ca2+
-
at the dimer interface coordinated by eight oxygen atoms, Ser87, Thr89 from both monomers, and two water molecules
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+
-
two-iron superoxide reductase with a ferrous active site
Fe2+
-
Zn/Fe-superoxide reductase
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+
-
1Fe-SOR or neelaredoxin class of superoxide reductases
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+
complex formation, kinetics, and electrochemistry, 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+
-
non-heme [Fe(His)4Cys] active sites
Fe2+
Treponema palladium
-
complex formation, kinetics, and electrochemistry, overview
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+
-
-
Fe2+/Fe3+
-
enzyme contains 1 iron atom/monomer
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+
-
0.5 iron atoms/mol subunit
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
Fe2+/Fe3+
-
center I is missing
Iron
-
0.8 atoms per subunit for wild-type, mutant E12V, 1.2 atoms per subunit, mutant E12Q, 0.9 atoms per subunit
Iron
2.3 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 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
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
-
contains 0.95 atoms of Fe per monomer
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 [4Fe4S] 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
-
Fe(His)4(cys) active centre
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
Zn2+
-
Zn/Fe-superoxide reductase
Zn2+
-
approx. 0.25 atoms/subunit
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
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evolution
-
Giardia trophozoite expresses an enzyme probably acquired from a prokaryote by lateral gene transfer. 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
evolution
-
the enzyme belongs to the class I superoxide reductase family
evolution
Megalodesulfovibrio gigas
-
the enzyme belongs to the class II superoxide reductase family
evolution
based on the number of metal centres, superoxide reductases can be divided into two major subclasses: neelaredoxins (Nlr) solely contain the active site (1Fe-SOR), while desulfoferrodoxins (Dfx) harbour an additional rubredoxin-like iron centre (2Fe-SOR)
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
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
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
evolution
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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
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
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
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
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
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
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
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
evolution
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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
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evolution
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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
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evolution
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based on the number of metal centres, superoxide reductases can be divided into two major subclasses: neelaredoxins (Nlr) solely contain the active site (1Fe-SOR), while desulfoferrodoxins (Dfx) harbour an additional rubredoxin-like iron centre (2Fe-SOR)
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evolution
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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
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evolution
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Giardia trophozoite expresses an enzyme probably acquired from a prokaryote by lateral gene transfer. 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
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evolution
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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
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evolution
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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
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evolution
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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
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evolution
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the enzyme belongs to the class I superoxide reductase family
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malfunction
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the enzyme-inactivated 1754M strain is significantly more air-sensitive than the wild-type strain on NOS agarose plates exposed to air
malfunction
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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
malfunction
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the enzyme-inactivated 1754M strain is significantly more air-sensitive than the wild-type strain on NOS agarose plates exposed to air
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malfunction
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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
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metabolism
the enzyme is involved in ROS detoxification
metabolism
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the enzyme is involved in ROS detoxification
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physiological function
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SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
Megalodesulfovibrio gigas
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SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
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SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
-
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
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SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
physiological function
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SOR is responsible for reductive eliminatioon of toxic superoxide as part of the detoxifying system
physiological function
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superoxide reductase is involved in superoxide detoxification
physiological function
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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 reductases play a key role in defence mechanisms against toxic oxygen species. SOR is responsible for scavenging toxic superoxide anion radicals, catalysing the one-electron reduction of superoxide to hydrogen peroxide
physiological function
-
the neelaredoxin-type SOR keeps toxic oxygen species levels under control. SORs are involved in scavenging superoxide radicals from the cell by catalyzing the reduction of superoxide to hydrogen peroxide
physiological function
-
Giardia trophozoite expresses a SOR possibly involved in superoxide detoxification
physiological function
-
superoxide reductase from the air-sensitive oral spirochete Treponema denticola is a principal enzymatic scavenger of superoxide in this organism, role for the enzyme in oxidative stress protection of O2-exposed Treponema denticola 35405
physiological function
the enzyme may contributes to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
physiological function
-
enzyme SOR efficiently detoxifies reactive oxygen species. Overexpression of SOD can improve the tolerance of transgenic organisms to various oxidative stresses
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
physiological function
superoxide reductase (SOR) affords protection from oxidative stress by reducing the superoxide anion to hydrogen peroxide
physiological function
-
the enzyme may contributes to the protection of cells from oxygen radicals formed by flavoproteins during periodic exposure to oxygen in natural environments
-
physiological function
-
Giardia trophozoite expresses a SOR possibly involved in superoxide detoxification
-
physiological function
-
superoxide reductase from the air-sensitive oral spirochete Treponema denticola is a principal enzymatic scavenger of superoxide in this organism, role for the enzyme in oxidative stress protection of O2-exposed Treponema denticola 35405
-
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
-
physiological function
-
SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system
-
additional information
-
SORs can be classified as 1Fe-SORs, or neelaredoxins, or as 2Fe-SORs, or desulfoferrodoxins, according to the number of metal centres. Both share a common active site in which the reduction of superoxide anion occurs. This site is composed of a pentacoordinated iron with four equatorial histidine imidazoles and one axial cysteine sulfur in a square-pyramidal geometry [Fe(Cys)(His)4]
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
-
direct electron transfer measurements, in the presence of superoxide anion, overview
additional information
Megalodesulfovibrio gigas
-
model structure of SOR-rubredoxin complex, docking simulations, overview
additional information
-
pH dependent ligand exchange in the final intermediate, overview
additional information
-
the enzyme contains non-heme [Fe(His)4Cys] active sites, homology structural modeling using the Tp SOR structure, PDB ID 1Y07, as template, overview
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
iron reduction does not lead to dissociation of glutamate from the catalytic metal or other structural changes, but the glutamate ligand undergoes X-ray-induced chemical changes, revealing high sensitivity of the GiSOR active site to X-ray radiation damage, enzyme structure modeling and structure comparisons
additional information
-
iron reduction does not lead to dissociation of glutamate from the catalytic metal or other structural changes, but the glutamate ligand undergoes X-ray-induced chemical changes, revealing high sensitivity of the GiSOR active site to X-ray radiation damage, enzyme structure modeling and structure comparisons
additional information
key catalytic residue is E23, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112
additional information
key catalytic residue is K9, catalytic Fe2+ binding residues are H10, H35, H41, C97, and H100
additional information
-
key catalytic residues are E12 and K13, catalytic Fe2+ binding residues are H14, H40, H46, C110, and H113
additional information
key catalytic residues are E12 and K13, catalytic Fe2+ binding residues are H14, H40, H46, C110, and H113
additional information
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114
additional information
-
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114
additional information
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114
additional information
-
key catalytic residues are E15 and K16, catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118
additional information
key catalytic residues are E15 and K16, catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118
additional information
key catalytic residues are E23, K24, H25, H50, H56, C111, and H114
additional information
-
key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118
additional information
-
key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118
additional information
key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118
additional information
key catalytic residues are E48, K40, H50, H70, H76, C119, and H122
additional information
Superoxide reductases form a group of non-heme iron enzymes that supply one electron during substrate reduction. In the ferrous state, the active site iron is coordinated by four equatorial histidines and an axial cysteinate, forming a square pyramidal geometry with a vacant site for substrate binding. In the octahedral ferric state, coordination of the active site is not uniform: during turnover, the sixth coordination site is supposedly occupied by dioxygen species in different protonation and oxidation states. In contrast, the ferric resting state comprises an additional glutamate as a ligand in most, but not all, cases. Metal binding site and active site structure analysis, overview
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
additional information
-
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114
-
additional information
-
key catalytic residue is E23, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112
-
additional information
-
Superoxide reductases form a group of non-heme iron enzymes that supply one electron during substrate reduction. In the ferrous state, the active site iron is coordinated by four equatorial histidines and an axial cysteinate, forming a square pyramidal geometry with a vacant site for substrate binding. In the octahedral ferric state, coordination of the active site is not uniform: during turnover, the sixth coordination site is supposedly occupied by dioxygen species in different protonation and oxidation states. In contrast, the ferric resting state comprises an additional glutamate as a ligand in most, but not all, cases. Metal binding site and active site structure analysis, overview
-
additional information
-
key catalytic residues are E14 and K15, catalytic Fe2+ binding residues are H16, H41, H47, C111, and H114
-
additional information
-
pH dependent ligand exchange in the final intermediate, overview
-
additional information
-
the enzyme contains non-heme [Fe(His)4Cys] active sites, homology structural modeling using the Tp SOR structure, PDB ID 1Y07, as template, overview
-
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
-
additional information
-
key catalytic residues are E47 and K48, catalytic Fe2+ binding residues are H49, H69, H74, C115, and H118
-
additional information
-
key catalytic residues are E15 and K16, catalytic Fe2+ binding residues are H17, H45, H51, C115, and H118
-
additional information
-
key catalytic residues are E48, K40, H50, H70, H76, C119, and H122
-
additional information
-
direct electron transfer measurements, in the presence of superoxide anion, overview
-
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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
E46A
site-directed mutagenesis, crystal structure determination
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
K48A
-
redox properties of the mutant compared to the wild-type enzyme
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
-
E46A
-
site-directed mutagenesis, crystal structure determination
-
E47A
-
site-directed mutagenesis, crystal structure determination
-
K48I
-
site-directed mutagenesis
-
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
-
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
-
E47A
-
site-directed mutagenesis
E48A
-
site-directed mutagenesis
E48A
-
site-directed mutagenesis
E23A
site-directed mutagenesis
T24K
site-directed mutagenesis
E23A
-
site-directed mutagenesis
-
T24K
-
site-directed mutagenesis
-
P8E
-
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
E48A
site-directed mutagenesis
K48A
-
redox properties of the mutant compared to the wild-type enzyme
E48A
-
site-directed mutagenesis
-
E12Q
site-directed mutagenesis
E12Q
-
mutation in corrdination site of iron. Detailed kinetic analysis
E12Q
-
lacking the highly conserved glutamate residue of the active site without profound influence on the iron binding behaviour
E12V
site-directed mutagenesis
E12V
-
mutation in corrdination site of iron. Detailed kinetic analysis
E12V
-
lacking the highly conserved glutamate residue of the active site without profound influence on the iron binding behaviour
E12V
-
redox properties of the mutant compared to the wild-type enzyme
E114A
-
crystal structure
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
-
mutation has almost no effect on the reaction with superoxide
E47A
-
active site of the mutant can transiently stabilize an Fe3+ peroxo species
E47A
crystallization data
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
site-directed mutagenesis, crystal structure determination
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
E47A
comparison of wild-type and mutant transient intermdiates
E47A
-
redox properties of the mutant compared to the wild-type enzyme
K48I
site-directed mutagenesis
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
C13S
-
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
C13S
-
mutant enzyme kinetics in comparison to the wild-type enzyme
E47A
-
-
E47A
-
site-directed mutagenesis
E47A
-
E47 may interact with the iron atom of ferric center II, most likely by carboxylate ligation
E47A
-
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
-
redox properties of the mutant compared to the wild-type enzyme
K48A
-
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
-
mutant enzyme kinetics in comparison to the wild-type enzyme
K48A
-
redox properties of the mutant compared to the wild-type enzyme
additional information
-
the mutant enzymes lacking the glutamate and lysine residues close to the active site can be a competent superoxide reductase
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
additional information
-
construction of inactive 1754M strain containing the insertionally inactivated Td SOR gene
additional information
-
construction of inactive 1754M strain containing the insertionally inactivated Td SOR gene
-
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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
brenda
Jovanovic, T.; Ascenso, C.; Hazlett, K.R.O.; Sikkink, R.; Krebs, C.; Litwiller, R.; Benson, L.M.; Moura, I.; Moura, J.J.G.; Radolf, J.D.; Huynh, B.H.; Naylor, S.; Rusnak, F.
Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase
J. Biol. Chem.
275
28439-28448
2000
Treponema pallidum
brenda
Lombard, M.; Fontecave, M.; Touati, D.; Niviere, V.
Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity
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275
115-121
2000
Desulfarculus baarsii
brenda
Abreu, I.A.; Saraiva, L.M.; Carita, J.; Huber, H.; Stetter, K.O.; Cabelli, D.; Teixeira, M.
Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by Neelaredoxin
Mol. Microbiol.
38
322-334
2000
Archaeoglobus fulgidus
brenda
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
brenda
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
brenda
Coulter, E.D.; Kurtz, D.M., Jr.
A role for rubredoxin in oxidative stress protection in Desulfovibrio vulgaris: catalytic electron transfer to rubrerythrin and two-iron superoxide reductase
Arch. Biochem. Biophys.
394
76-86
2001
Desulfovibrio vulgaris
brenda
Lumppio, H.L.; Shenvi, N.V.; Summers, A.O.; Voordouw, G.; Kurtz, D.M., Jr.
Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: a novel oxidative stress protection system
J. Bacteriol.
183
101-108
2001
Desulfovibrio vulgaris
brenda
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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
brenda
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
brenda
Coulter, E.D.; Emerson, J.P.; Kurtz, D.M., Jr.; Cabelli, D.E.
Superoxide reactivity of rubredoxin oxidoreductase (desulfoferrodoxin) from Desulfovibrio vulgaris: a pulse radiolysis study
J. Am. Chem. Soc.
122
11555-11556
2000
Desulfovibrio vulgaris
-
brenda
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
brenda
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Superoxide reductase from Desulfoarculus baarsii
Methods Enzymol.
349
123-129
2002
Desulfarculus baarsii, Treponema pallidum
brenda
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Kinetics and mechanism of superoxide reduction by two-iron superoxide reductase from Desulfovibrio vulgaris
Biochemistry
41
4348-4357
2002
Desulfovibrio vulgaris
brenda
Rodrigues, J.V.; Abreu, I.A.; Saraiva, L.M.; Teixeira, M.
Rubredoxin acts as an electron donor for neelaredoxin in Archaeoglobus fulgidus
Biochem. Biophys. Res. Commun.
329
1300-1305
2005
Archaeoglobus fulgidus
brenda
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
brenda
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
brenda
Emerson, J.P.; Cabelli, D.E.; Kurtz, D.M., Jr.
An engineered two-iron superoxide reductase lacking the [Fe(SCys)4] site retains its catalytic properties in vitro and in vivo
Proc. Natl. Acad. Sci. USA
100
3802-3807
2003
Desulfovibrio vulgaris
brenda
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
brenda
Santos-Silva, T.; Trincao, J.; Carvalho, A.L.; Bonifacio, C.; Auchere, F.; Moura, I.; Moura, J.J.; Romao, M.J.
Superoxide reductase from the syphilis spirochete Treponema pallidum: crystallization and structure determination using soft X-rays
Acta Crystallogr. Sect. F
61
967-970
2005
Treponema pallidum
brenda
Rodrigues, J.V.; Abreu, I.A.; Cabelli, D.; Teixeira, M.
Superoxide reduction mechanism of Archaeoglobus fulgidus one-iron superoxide reductase
Biochemistry
45
9266-9278
2006
Archaeoglobus fulgidus
brenda
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
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119
38-48
2006
Desulfarculus baarsii, Treponema pallidum
brenda
Im, Y.J.; Ji, M.; Lee, A.M.; Boss, W.F.; Grunden, A.M.
Production of a thermostable archaeal superoxide reductase in plant cells
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2005
Pyrococcus furiosus
brenda
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Role of protons in superoxide reduction by a superoxide reductase analogue
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44
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2005
synthetic construct
brenda
Mathe, C.; Niviere, V.; Mattioli, T.A.
Fe3+-hydroxide ligation in the superoxide reductase from Desulfoarculus baarsii is associated with pH dependent spectral changes
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2005
Desulfarculus baarsii
brenda
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The first crystal structure of class III superoxide reductase from Treponema pallidum
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11
548-558
2006
Treponema pallidum
brenda
Rodrigues, J.V.; Saraiva, L.M.; Abreu, I.A.; Teixeira, M.; Cabelli, D.E.
Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: comparison with neelaredoxin
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2007
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O29903)
brenda
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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
brenda
Kovacs, J.A.; Brines, L.M.
Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase
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40
501-509
2007
Desulfarculus baarsii (Q46495)
brenda
Huang, V.W.; Emerson, J.P.; Kurtz, D.M.
Reaction of Desulfovibrio vulgaris two-iron superoxide reductase with superoxide: insights from stopped-flow spectrophotometry
Biochemistry
46
11342-11351
2007
Desulfovibrio vulgaris
brenda
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Superoxide reductases
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2007
2569-2581
2007
Desulfovibrio desulfuricans, Megalodesulfovibrio gigas, Methanothermobacter thermautotrophicus, Treponema pallidum, Archaeoglobus fulgidus (O29903), Desulfovibrio vulgaris (P20418), Pyrococcus furiosus (P82385), Desulfarculus baarsii (Q46495), Thermotoga maritima (Q9WZC6)
-
brenda
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)
-
brenda
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Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase
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581
5605-5610
2007
Clostridium acetobutylicum (Q97GB9), Clostridium acetobutylicum
brenda
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Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on superoxide reductase: role of the axial thiolate in reactivity
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129
12418-12431
2007
Pyrococcus furiosus (P82385), Pyrococcus furiosus
brenda
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Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii
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282
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2007
Desulfarculus baarsii (Q46495), Desulfarculus baarsii
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Rodrigues, J.V.; Victor, B.L.; Huber, H.; Saraiva, L.M.; Soares, C.M.; Cabelli, D.E.; Teixeira, M.
Superoxide reduction by Nanoarchaeum equitans neelaredoxin, an enzyme lacking the highly conserved glutamate iron ligand
J. Biol. Inorg. Chem.
13
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2008
Nanoarchaeum equitans
brenda
Todorovic, S.; Rodrigues, J.V.; Pinto, A.F.; Thomsen, C.; Hildebrandt, P.; Teixeira, M.; Murgida, D.H.
Resonance Raman study of the superoxide reductase from Archaeoglobus fulgidus, E12 mutants and a natural variant
Phys. Chem. Chem. Phys.
11
1809-1815
2009
Archaeoglobus fulgidus, Nanoarchaeum equitans
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Bandeiras, T.M.; Romao, C.V.; Rodrigues, J.V.; Teixeira, M.; Matias, P.M.
Purification, crystallization and X-ray crystallographic analysis of Archaeoglobus fulgidus neelaredoxin
Acta Crystallogr. Sect. F
66
316-319
2010
Archaeoglobus fulgidus
brenda
Pinho, F.G.; Romao, C.V.; Pinto, A.F.; Saraiva, L.M.; Huber, H.; Matias, P.M.; Teixeira, M.; Bandeiras, T.M.
Cloning, purification, crystallization and X-ray crystallographic analysis of Ignicoccus hospitalis neelaredoxin
Acta Crystallogr. Sect. F
66
605-607
2010
Ignicoccus hospitalis
brenda
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, Megalodesulfovibrio gigas, Desulfovibrio vulgaris, Treponema pallidum, Nanoarchaeum equitans, Pyrococcus horikoshii (O58810), Desulfovibrio desulfuricans (P22076), Pyrococcus furiosus (P82385), Thermotoga maritima (Q9WZC6), Pyrococcus horikoshii OT-3 (O58810)
brenda
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
brenda
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
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2011
Desulfarculus baarsii
brenda
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
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2005
Pyrococcus furiosus
brenda
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
brenda
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
brenda
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
brenda
Folgosa, F.; Cordas, C.M.; Santos, J.A.; Pereira, A.S.; Moura, J.J.; Tavares, P.; Moura, I.
New spectroscopic and electrochemical insights on a class I superoxide reductase: evidence for an intramolecular electron-transfer pathway
Biochem. J.
438
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2011
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
Caranto, J.D.; Gebhardt, L.L.; MacGowan, C.E.; Limberger, R.J.; Kurtz, D.M.
Treponema denticola superoxide reductase: in vivo role, in vitro reactivities, and a novel [Fe(Cys)(4)] site
Biochemistry
51
5601-5610
2012
Treponema denticola, Treponema denticola 35405
brenda
Almeida, R.M.; Turano, P.; Moura, I.; Moura, J.J.; Pauleta, S.R.
Superoxide reductase: different interaction modes with its two redox partners
ChemBioChem
14
1858-1866
2013
Megalodesulfovibrio gigas
brenda
Krtzer, C.; Welte, C.; Drner, K.; Friedrich, T.; Deppenmeier, U.
Methanoferrodoxin represents a new class of superoxide reductase containing an iron-sulfur cluster
FEBS J.
278
442-451
2011
Methanosarcina mazei (Q8PZ62), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PZ62)
brenda
Testa, F.; Mastronicola, D.; Cabelli, D.E.; Bordi, E.; Pucillo, L.P.; Sarti, P.; Saraiva, L.M.; Giuffre, A.; Teixeira, M.
The superoxide reductase from the early diverging eukaryote Giardia intestinalis
Free Radic. Biol. Med.
51
1567-1574
2011
Giardia intestinalis, Giardia intestinalis WB clone C6
brenda
Pinto, A.F.; Romao, C.V.; Pinto, L.C.; Huber, H.; Saraiva, L.M.; Todorovic, S.; Cabelli, D.; Teixeira, M.
Superoxide reduction by a superoxide reductase lacking the highly conserved lysine residue
J. Biol. Inorg. Chem.
20
155-164
2015
Ignicoccus hospitalis
brenda
Horch, M.; Pinto, A.F.; Utesch, T.; Mroginski, M.A.; Romao CV, Teixeira M, Hildebrandt P, Zebger I.
Reductive activation and structural rearrangement in superoxide reductase: a combined infrared spectroscopic and computational study
Phys. Chem. Chem. Phys.
16
14220-14230
2014
Ignicoccus hospitalis
brenda
Sousa, C.M.; Carpentier, P.; Matias, P.M.; Testa, F.; Pinho, F.; Sarti, P.; Giuffre, A.; Bandeiras, T.M.; Romao, C.V.
Superoxide reductase from Giardia intestinalis structural characterization of the first SOR from a eukaryotic organism shows an iron centre that is highly sensitive to photoreduction
Acta Crystallogr. Sect. D
71
2236-2247
2015
Giardia intestinalis (V6TJK7), Giardia intestinalis
brenda
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
brenda
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), Desulfovibrio desulfuricans, Desulfovibrio vulgaris, Dosidicus gigas, Ignicoccus hospitalis (A8AC72), Pyrococcus horikoshii (O58810), Treponema pallidum (O82795), Pyrococcus furiosus (P82385), Desulfarculus baarsii (Q46495), Nanoarchaeum equitans (Q74MF3), Thermotoga maritima (Q9WZC6), Archaeoglobus fulgidus ATCC 49558 (O29903), Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 (A8AC72), Pyrococcus furiosus ATCC 43587 (P82385), Desulfarculus baarsii ATCC 33931 (Q46495), Thermotoga maritima ATCC 43589 (Q9WZC6), Treponema pallidum Nichols (O82795)
brenda
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
brenda
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.
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716-724
2001
Pyrococcus furiosus (P82385)
brenda
Horch, M.; Pinto, A.; Mroginski, M.; Teixeira, M.; Hildebrandt, P.; Zebger, I.
Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase
RSC Adv.
4
54091-54095
2014
Ignicoccus hospitalis (A8AC72), Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 (A8AC72)
-
brenda
Lakhal, R.; Auria, R.; Davidson, S.; Ollivier, B.; Durand, M.; Dolla, A.; Hamdi, M.; Combet-Blanc, Y.
Oxygen uptake rates in the hyperthermophilic anaerobe Thermotoga maritima grown in a bioreactor under controlled oxygen exposure Clues to its defence strategy against oxidative stress
Arch. Microbiol.
193
429-438
2011
Thermotoga maritima (Q9WZC6), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WZC6)
brenda