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Literature summary for 1.15.1.2 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)

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

Crystallization (Commentary)

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

Metals/Ions

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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced rubredoxin + superoxide + H+ Methanothermobacter thermautotrophicus
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Desulfovibrio desulfuricans
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Megalodesulfovibrio gigas
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Treponema pallidum
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Pyrococcus furiosus
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Archaeoglobus fulgidus
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Desulfarculus baarsii
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Desulfovibrio vulgaris
-
rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ Thermotoga maritima
-
rubredoxin + H2O2
-
?

Organism

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information structure-function relationship, overview Methanothermobacter thermautotrophicus ?
-
?
additional information structure-function relationship, overview Desulfovibrio desulfuricans ?
-
?
additional information structure-function relationship, overview Megalodesulfovibrio gigas ?
-
?
additional information structure-function relationship, overview Treponema pallidum ?
-
?
additional information structure-function relationship, overview Pyrococcus furiosus ?
-
?
additional information structure-function relationship, overview Archaeoglobus fulgidus ?
-
?
additional information structure-function relationship, overview Desulfarculus baarsii ?
-
?
additional information structure-function relationship, overview Desulfovibrio vulgaris ?
-
?
additional information structure-function relationship, overview Thermotoga maritima ?
-
?
reduced rubredoxin + superoxide + H+
-
Methanothermobacter thermautotrophicus rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Desulfovibrio desulfuricans rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Megalodesulfovibrio gigas rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Treponema pallidum rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Pyrococcus furiosus rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Archaeoglobus fulgidus rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Desulfarculus baarsii rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Desulfovibrio vulgaris rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+
-
Thermotoga maritima rubredoxin + H2O2
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
reduced rubredoxin + superoxide + H+ mechanistic aspects of biological superoxide anion reduction, overview Methanothermobacter thermautotrophicus rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ mechanistic aspects of biological superoxide anion reduction, overview Megalodesulfovibrio gigas rubredoxin + H2O2
-
?
reduced rubredoxin + superoxide + H+ mechanistic aspects of biological superoxide anion reduction, overview Archaeoglobus fulgidus rubredoxin + H2O2
-
?

Subunits

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
reduced rubredoxin
-
Methanothermobacter thermautotrophicus
reduced rubredoxin
-
Desulfovibrio desulfuricans
reduced rubredoxin
-
Megalodesulfovibrio gigas
reduced rubredoxin
-
Treponema pallidum
reduced rubredoxin
-
Archaeoglobus fulgidus
reduced rubredoxin
-
Desulfarculus baarsii
reduced rubredoxin
-
Thermotoga maritima
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
reduced rubredoxin encoded by gene rub Desulfovibrio vulgaris