Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Pereira, A.S.; Tavares, P.; Folgosa, F.; Almeida, R.M.; Moura, I.; Moura, J.J.
    Superoxide reductases (2007), Eur. J. Inorg. Chem., 2007, 2569-2581.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.2 expression of class I Dfx, phylogenetic analysis Methanothermobacter thermautotrophicus
1.15.1.2 expression of class I Dfx, phylogenetic analysis Desulfarculus baarsii
1.15.1.2 expression of class II Nlr and of class I Dfx, phylogenetic analysis Archaeoglobus fulgidus
1.15.1.2 expression of class II Nlr, phylogenetic analysis Pyrococcus furiosus
1.15.1.2 expression of class II Nlr, phylogenetic analysis Thermotoga maritima
1.15.1.2 expression of class III enzyme in Escherichia coli, phylogenetic analysis Treponema pallidum
1.15.1.2 gene dsr, expression of class II Nlr in Escherichia coli, phylogenetic analysis Megalodesulfovibrio gigas
1.15.1.2 gene rbo, expression of class I Dfx, phylogenetic analysis Desulfovibrio vulgaris
1.15.1.2 phylogenetic analysis Desulfovibrio desulfuricans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.2 crystallization of the native enzyme, X-ray diffraction structure determination and analysis at 1.9 A resolution, modelling Desulfovibrio desulfuricans
1.15.1.2 crystallization of the recombinant and the native enzyme Pyrococcus furiosus
1.15.1.2 crystallization of the recombinant enzyme Treponema pallidum
1.15.1.2 crystallization of the recombinant enzyme Desulfarculus baarsii
1.15.1.2 crystallization of the recombinant enzyme Thermotoga maritima

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.2 Ca2+ at the dimer interface coordinated by eight oxygen atoms, Ser87, Thr89 from both monomers, and two water molecules Desulfovibrio desulfuricans
1.15.1.2 Fe2+ the class I enzyme contains two iron-centers, binding structure, overview Methanothermobacter thermautotrophicus
1.15.1.2 Fe2+ the class I enzyme contains two iron-centers, binding structure, overview Desulfarculus baarsii
1.15.1.2 Fe2+ the class I enzyme contains two iron-centers, binding structure, overview Desulfovibrio vulgaris
1.15.1.2 Fe2+ the class I enzyme contains two iron-centers, i.e. two iron atoms per subunit, binding structure, overview Desulfovibrio desulfuricans
1.15.1.2 Fe2+ the class I enzyme contains two iron-centers, while the class II enzyme contains one iron-center, binding structure, overview Archaeoglobus fulgidus
1.15.1.2 Fe2+ the class II enzyme contains one iron-center, binding structure, overview Megalodesulfovibrio gigas
1.15.1.2 Fe2+ the class II enzyme contains one iron-center, binding structure, overview Thermotoga maritima
1.15.1.2 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 Pyrococcus furiosus
1.15.1.2 Fe2+ the class III enzyme contains one iron-center, a homodimer containing a sole iron site per monomer, binding structure, overview Treponema pallidum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.15.1.2 14000
-
 2 * 14000 Desulfovibrio desulfuricans
1.15.1.2 14000
-
 2 * 14000, a homodimer Treponema pallidum

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 + H+ Methanothermobacter thermautotrophicus
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Desulfovibrio desulfuricans
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Megalodesulfovibrio gigas
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Treponema pallidum
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Pyrococcus furiosus
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Archaeoglobus fulgidus
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Desulfarculus baarsii
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Desulfovibrio vulgaris
-
 rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ Thermotoga maritima
-
 rubredoxin + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.2 Archaeoglobus fulgidus O29903
-
-
1.15.1.2 Desulfarculus baarsii Q46495
-
-
1.15.1.2 Desulfovibrio desulfuricans
-
 strain ATCC 27774
-
1.15.1.2 Desulfovibrio vulgaris P20418 var. Hildenborough, gene rbo
-
1.15.1.2 Megalodesulfovibrio gigas
-
 gene dsr
-
1.15.1.2 Methanothermobacter thermautotrophicus
-
-
-
1.15.1.2 Pyrococcus furiosus P82385
-
-
1.15.1.2 Thermotoga maritima Q9WZC6
-
-
1.15.1.2 Treponema pallidum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Methanothermobacter thermautotrophicus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Desulfovibrio desulfuricans
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Megalodesulfovibrio gigas
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Treponema pallidum
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Pyrococcus furiosus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Archaeoglobus fulgidus
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Desulfarculus baarsii
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Desulfovibrio vulgaris
a
1.15.1.2 superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin enzyme active site structure and mechanism Thermotoga maritima
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.2 additional information structure-function relationship, overview Methanothermobacter thermautotrophicus ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Desulfovibrio desulfuricans ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Megalodesulfovibrio gigas ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Treponema pallidum ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Pyrococcus furiosus ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Archaeoglobus fulgidus ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Desulfarculus baarsii ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Desulfovibrio vulgaris ?
-
 ?
1.15.1.2 additional information structure-function relationship, overview Thermotoga maritima ?
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Methanothermobacter thermautotrophicus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Desulfovibrio desulfuricans rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Megalodesulfovibrio gigas rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Treponema pallidum rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Pyrococcus furiosus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Archaeoglobus fulgidus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Desulfarculus baarsii rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Desulfovibrio vulgaris rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+
-
 Thermotoga maritima rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ functionally important residues are Glu14, Lys15, His16, His41, His51, His118, Ile49, and Cys111, mechanistic aspects of biological superoxide anion reduction, overview Pyrococcus furiosus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ functionally important residues are Glu15, Lys16, His17, His45, His51, His118, Ile53, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview Thermotoga maritima rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ functionally important residues are Glu46, Lys47, His48, His68, His74, His118, Ile76, and Cys115, mechanistic aspects of biological superoxide anion reduction, overview Desulfovibrio desulfuricans rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ functionally important residues are Glu47, Lys48, His49, His69, His75, His119, Ile77, and Cys116, mechanistic aspects of biological superoxide anion reduction, overview Desulfarculus baarsii rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ functionally important residues are Glu47, Lys48, His49, His69, His75, His119, Ile77, and Cys116, mechanistic aspects of biological superoxide anion reduction, overview Desulfovibrio vulgaris rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ functionally important residues are Glu48, Lys49, His50, His70, His76, His122, Ile78, and Cys119, mechanistic aspects of biological superoxide anion reduction, overview Treponema pallidum rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ mechanistic aspects of biological superoxide anion reduction, overview Methanothermobacter thermautotrophicus rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ mechanistic aspects of biological superoxide anion reduction, overview Megalodesulfovibrio gigas rubredoxin + H2O2
-
 ?
1.15.1.2 reduced rubredoxin + superoxide + H+ mechanistic aspects of biological superoxide anion reduction, overview Archaeoglobus fulgidus rubredoxin + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.2 dimer 2 * 14000 Desulfovibrio desulfuricans
1.15.1.2 dimer 2 * 14000, a homodimer Treponema pallidum
1.15.1.2 More structure-function relationship, overview Methanothermobacter thermautotrophicus
1.15.1.2 More structure-function relationship, overview Desulfovibrio desulfuricans
1.15.1.2 More structure-function relationship, overview Treponema pallidum
1.15.1.2 More structure-function relationship, overview Archaeoglobus fulgidus
1.15.1.2 More structure-function relationship, overview Desulfarculus baarsii
1.15.1.2 More structure-function relationship, overview Desulfovibrio vulgaris
1.15.1.2 More structure-function relationship, overview Thermotoga maritima
1.15.1.2 More primary structure, structure-function relationship, overview Megalodesulfovibrio gigas
1.15.1.2 More primary structure, structure-function relationship, overview Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
1.15.1.2 desulfoferrodoxin
-
 Desulfovibrio desulfuricans
1.15.1.2 desulfoferrodoxin
-
 Archaeoglobus fulgidus
1.15.1.2 desulfoferrodoxin
-
 Desulfarculus baarsii
1.15.1.2 desulfoferrodoxin
-
 Desulfovibrio vulgaris
1.15.1.2 Dfx
-
 Desulfovibrio desulfuricans
1.15.1.2 Dfx
-
 Archaeoglobus fulgidus
1.15.1.2 Dfx
-
 Desulfarculus baarsii
1.15.1.2 Dfx
-
 Desulfovibrio vulgaris
1.15.1.2 More Dfx belongs to the class I of superoxide reductases, while Nlr belongs to the class II superoxide reductases Archaeoglobus fulgidus
1.15.1.2 More the enzyme belongs to the class I of superoxide reductases Desulfovibrio desulfuricans
1.15.1.2 More the enzyme belongs to the class I of superoxide reductases Desulfarculus baarsii
1.15.1.2 More the enzyme belongs to the class I of superoxide reductases Desulfovibrio vulgaris
1.15.1.2 More the enzyme belongs to the class II of superoxide reductases Methanothermobacter thermautotrophicus
1.15.1.2 More the enzyme belongs to the class II of superoxide reductases Megalodesulfovibrio gigas
1.15.1.2 More the enzyme belongs to the class II of superoxide reductases Pyrococcus furiosus
1.15.1.2 More the enzyme belongs to the class II of superoxide reductases Thermotoga maritima
1.15.1.2 More the enzyme belongs to the class III of superoxide reductases Treponema pallidum
1.15.1.2 neelaredoxin
-
 Methanothermobacter thermautotrophicus
1.15.1.2 neelaredoxin
-
 Megalodesulfovibrio gigas
1.15.1.2 neelaredoxin
-
 Treponema pallidum
1.15.1.2 neelaredoxin
-
 Pyrococcus furiosus
1.15.1.2 neelaredoxin
-
 Archaeoglobus fulgidus
1.15.1.2 neelaredoxin
-
 Thermotoga maritima
1.15.1.2 Nlr
-
 Methanothermobacter thermautotrophicus
1.15.1.2 Nlr
-
 Megalodesulfovibrio gigas
1.15.1.2 Nlr
-
 Treponema pallidum
1.15.1.2 Nlr
-
 Pyrococcus furiosus
1.15.1.2 Nlr
-
 Archaeoglobus fulgidus
1.15.1.2 Nlr
-
 Thermotoga maritima
1.15.1.2 rubredoxin oxidoreductase
-
 Methanothermobacter thermautotrophicus
1.15.1.2 rubredoxin oxidoreductase
-
 Desulfovibrio desulfuricans
1.15.1.2 rubredoxin oxidoreductase
-
 Megalodesulfovibrio gigas
1.15.1.2 rubredoxin oxidoreductase
-
 Treponema pallidum
1.15.1.2 rubredoxin oxidoreductase
-
 Pyrococcus furiosus
1.15.1.2 rubredoxin oxidoreductase
-
 Archaeoglobus fulgidus
1.15.1.2 rubredoxin oxidoreductase
-
 Desulfarculus baarsii
1.15.1.2 rubredoxin oxidoreductase
-
 Desulfovibrio vulgaris
1.15.1.2 rubredoxin oxidoreductase
-
 Thermotoga maritima
1.15.1.2 SOR
-
 Methanothermobacter thermautotrophicus
1.15.1.2 SOR
-
 Desulfovibrio desulfuricans
1.15.1.2 SOR
-
 Megalodesulfovibrio gigas
1.15.1.2 SOR
-
 Treponema pallidum
1.15.1.2 SOR
-
 Pyrococcus furiosus
1.15.1.2 SOR
-
 Archaeoglobus fulgidus
1.15.1.2 SOR
-
 Desulfarculus baarsii
1.15.1.2 SOR
-
 Desulfovibrio vulgaris
1.15.1.2 SOR
-
 Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
1.15.1.2 reduced rubredoxin
-
 Methanothermobacter thermautotrophicus
1.15.1.2 reduced rubredoxin
-
 Desulfovibrio desulfuricans
1.15.1.2 reduced rubredoxin
-
 Megalodesulfovibrio gigas
1.15.1.2 reduced rubredoxin
-
 Treponema pallidum
1.15.1.2 reduced rubredoxin
-
 Archaeoglobus fulgidus
1.15.1.2 reduced rubredoxin
-
 Desulfarculus baarsii
1.15.1.2 reduced rubredoxin
-
 Thermotoga maritima
1.15.1.2 reduced rubredoxin a potential Rd binding site is located in the vicinity of the solvent-exposed residues that are close to the iron centre Pyrococcus furiosus
1.15.1.2 reduced rubredoxin encoded by gene rub Desulfovibrio vulgaris