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Literature summary extracted from

  • Pinto, A.; Rodrigues, J.; Teixeira, M.
    Reductive elimination of superoxide: Structure and mechanism of superoxide reductases (2010), Biochim. Biophys. Acta, 1804, 285-297.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 cloning of the desulfoferrodoxin, encoded adjacent to a gene encoding a type I rubredoxin forming a single transcriptional unit Desulfovibrio vulgaris
1.15.1.2 DNA and amino acid sequence analysis, phylogenetic tree Archaeoglobus fulgidus
1.15.1.2 DNA and amino acid sequence analysis, phylogenetic tree Treponema pallidum
1.15.1.2 DNA and amino acid sequence analysis, phylogenetic tree Desulfarculus baarsii
1.15.1.2 DNA and amino acid sequence analysis, phylogenetic tree Nanoarchaeum equitans
1.15.1.2 DNA and amino acid sequence analysis, phylogenetic tree Pyrococcus furiosus
1.15.1.2 DNA and amino acid sequence analysis, phylogenetic tree Desulfovibrio desulfuricans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.2 crystal structure analysis of the native and ferricyanide bound wild-type enzyme, PDB ID 1DFX Desulfovibrio desulfuricans
1.15.1.2 crystal structure analysis of the native and Glu unbound wild-type enzyme, PDB ID 1Y07 Treponema pallidum
1.15.1.2 crystal structure analysis of the oxidized and Glu bound wild-type enzyme, PDB ID 2HVB Pyrococcus horikoshii
1.15.1.2 crystal structure analysis of the reduced or the oxidized and Glu bound wild-type enzyme, PDB IDs 1DQI, 1DO6, and 1DQK Pyrococcus furiosus
1.15.1.2 crystal structure analysis of the reduced wild-type enzyme, PDB ID 2AMU Thermotoga maritima
1.15.1.2 crystal structure analysis of the wild-type and E114A mutant enzymes in different oxidation states, PDB IDs 2JI3, 2JI2, 2JI1, and 1VZI Desulfarculus baarsii

Protein Variants

EC Number Protein Variants Comment Organism
1.15.1.2 E114A crystal structure Desulfarculus baarsii
1.15.1.2 E12V redox properties of the mutant compared to the wild-type enzyme Archaeoglobus fulgidus
1.15.1.2 E47A redox properties of the mutant compared to the wild-type enzyme Desulfovibrio vulgaris
1.15.1.2 E47A redox properties of the mutant compared to the wild-type enzyme Desulfarculus baarsii
1.15.1.2 K48A redox properties of the mutant compared to the wild-type enzyme Desulfovibrio vulgaris
1.15.1.2 K48A redox properties of the mutant compared to the wild-type enzyme Treponema pallidum
1.15.1.2 K48A redox properties of the mutant compared to the wild-type enzyme Desulfarculus baarsii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.15.1.2 additional information
-
 additional information steady-state kinetics Megalodesulfovibrio gigas

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 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 Archaeoglobus fulgidus
1.15.1.2 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 Treponema pallidum
1.15.1.2 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 Thermotoga maritima
1.15.1.2 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 Pyrococcus horikoshii
1.15.1.2 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 Pyrococcus furiosus
1.15.1.2 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 Desulfarculus baarsii
1.15.1.2 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 Desulfovibrio desulfuricans
1.15.1.2 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 Desulfovibrio vulgaris
1.15.1.2 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 Megalodesulfovibrio gigas
1.15.1.2 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 Nanoarchaeum equitans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Desulfovibrio vulgaris
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Archaeoglobus fulgidus
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Megalodesulfovibrio gigas
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Treponema pallidum
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Desulfarculus baarsii
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Nanoarchaeum equitans
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Pyrococcus furiosus
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Thermotoga maritima
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Pyrococcus horikoshii
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Desulfovibrio desulfuricans
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+ Pyrococcus horikoshii OT-3
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Archaeoglobus fulgidus
-
-
-
1.15.1.2 Desulfarculus baarsii
-
-
-
1.15.1.2 Desulfovibrio desulfuricans P22076
-
-
1.15.1.2 Desulfovibrio vulgaris
-
-
-
1.15.1.2 Megalodesulfovibrio gigas
-
-
-
1.15.1.2 Nanoarchaeum equitans
-
-
-
1.15.1.2 Pyrococcus furiosus P82385
-
-
1.15.1.2 Pyrococcus horikoshii O58810
-
-
1.15.1.2 Pyrococcus horikoshii OT-3 O58810
-
-
1.15.1.2 Thermotoga maritima Q9WZC6
-
-
1.15.1.2 Treponema pallidum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.2 isolation of center I and II Megalodesulfovibrio gigas

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, geometry of the catalytic center, oxidative cycle/reductive pathway, overview Pyrococcus furiosus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, geometry of the catalytic center, oxidative cycle/reductive pathway, overview Desulfovibrio desulfuricans
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Desulfovibrio vulgaris
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Archaeoglobus fulgidus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Megalodesulfovibrio gigas
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Treponema pallidum
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Desulfarculus baarsii
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Nanoarchaeum equitans
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Thermotoga maritima
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin reaction mechanism, oxidative cycle/reductive pathway, overview Pyrococcus horikoshii
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 additional information redox properties of SOR's catalytic center, overview Archaeoglobus fulgidus ?
-
 ?
1.15.1.2 additional information redox properties of SOR's catalytic center, overview Megalodesulfovibrio gigas ?
-
 ?
1.15.1.2 additional information redox properties of SOR's catalytic center, overview Treponema pallidum ?
-
 ?
1.15.1.2 additional information redox properties of SOR's catalytic center, overview Desulfarculus baarsii ?
-
 ?
1.15.1.2 additional information redox properties of SOR's catalytic center, overview Nanoarchaeum equitans ?
-
 ?
1.15.1.2 additional information redox properties of SOR's catalytic center, overview Desulfovibrio desulfuricans ?
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Desulfovibrio vulgaris rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Archaeoglobus fulgidus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Megalodesulfovibrio gigas rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Treponema pallidum rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Desulfarculus baarsii rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Nanoarchaeum equitans rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Pyrococcus furiosus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Thermotoga maritima rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Pyrococcus horikoshii rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Desulfovibrio desulfuricans rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + 2 H+
-
 Pyrococcus horikoshii OT-3 rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 homodimer
-
 Desulfarculus baarsii
1.15.1.2 homodimer the 1Fe-SOR from Treponema pallidum, which has an extra N-terminal domain reminiscent of those from 2Fe-SORs, is a homodimer Treponema pallidum
1.15.1.2 homodimer three-dimensional structure of SOR, overview Desulfovibrio desulfuricans
1.15.1.2 homotetramer
-
 Archaeoglobus fulgidus
1.15.1.2 homotetramer
-
 Nanoarchaeum equitans
1.15.1.2 homotetramer
-
 Thermotoga maritima
1.15.1.2 homotetramer
-
 Pyrococcus horikoshii
1.15.1.2 homotetramer 1Fe-SOR Pyrococcus furiosus
1.15.1.2 More three-dimensional structure of the neelaredoxin, overview Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 1Fe-SOR
-
 Archaeoglobus fulgidus
1.15.1.2 1Fe-SOR
-
 Treponema pallidum
1.15.1.2 1Fe-SOR
-
 Pyrococcus furiosus
1.15.1.2 1Fe-SOR
-
 Thermotoga maritima
1.15.1.2 1Fe-SOR
-
 Pyrococcus horikoshii
1.15.1.2 2Fe-SOR
-
 Archaeoglobus fulgidus
1.15.1.2 2Fe-SOR
-
 Desulfarculus baarsii
1.15.1.2 2Fe-SOR
-
 Desulfovibrio desulfuricans
1.15.1.2 Dfx
-
 Desulfovibrio desulfuricans
1.15.1.2 neelaredoxin
-
 Pyrococcus furiosus
1.15.1.2 SOR
-
 Desulfovibrio vulgaris
1.15.1.2 SOR
-
 Archaeoglobus fulgidus
1.15.1.2 SOR
-
 Megalodesulfovibrio gigas
1.15.1.2 SOR
-
 Treponema pallidum
1.15.1.2 SOR
-
 Desulfarculus baarsii
1.15.1.2 SOR
-
 Nanoarchaeum equitans
1.15.1.2 SOR
-
 Pyrococcus furiosus
1.15.1.2 SOR
-
 Thermotoga maritima
1.15.1.2 SOR
-
 Pyrococcus horikoshii
1.15.1.2 SOR
-
 Desulfovibrio desulfuricans

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 additional information structure of the neelaredoxin center, oxidized and reduced forms, overview Pyrococcus furiosus
1.15.1.2 additional information the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview Desulfovibrio vulgaris
1.15.1.2 additional information the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview Megalodesulfovibrio gigas
1.15.1.2 additional information the enzyme contains two iron sites: center I, similar to that of desulforedoxin, a small iron protein having a rubredoxin-like FeCys4 center, and center II, another type of iron site, which is named desulfoferrodoxin, Dfx, or rubredoxin. Structure of the FeCys4 center I, oxidized and reduced forms. overview Desulfovibrio desulfuricans

General Information

EC Number General Information Comment Organism
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Desulfovibrio vulgaris
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Megalodesulfovibrio gigas
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Treponema pallidum
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Desulfarculus baarsii
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Nanoarchaeum equitans
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Pyrococcus furiosus
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Thermotoga maritima
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Pyrococcus horikoshii
1.15.1.2 physiological function SOR is responsible for reductive elimination of toxic superoxide as part of the detoxifying system Desulfovibrio desulfuricans
1.15.1.2 physiological function SOR is responsible for reductive eliminatioon of toxic superoxide as part of the detoxifying system Archaeoglobus fulgidus