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Literature summary extracted from

  • Kolaj-Robin, O.; Noor, M.R.; OKane, S.R.; Baymann, F.; Soulimane, T.
    Atypical features of Thermus thermophilus succinate:quinone reductase (2013), PLoS ONE, 8, e53559.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.1 recombinant expression of C-terminally His6-tagged or N-termminally His8-tagged enzyme in Thermus thermophilus under the control of a constitutive promoter Thermus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 3-nitropropionic acid
-
Thermus thermophilus
1.3.5.1 malonate
-
Thermus thermophilus
1.3.5.1 nonyl-4-hydroxyquinoline-N-oxide the semiquinone analog and inhibitor of quinone reactions in complex II shows no influence on the redox behavior of the heme b moieties Thermus thermophilus
1.3.5.1 oxaloacetate
-
Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.1 additional information
-
additional information interprotomer temperature-dependent positive cooperativity in the trimeric complex. Only the trimer, not the monomer, exhibits positive cooperativity at high temperatures Thermus thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 membrane
-
Thermus thermophilus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 Fe2+ the enzyme contains a [3Fe-4S] center Thermus thermophilus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.5.1 119800
-
monomeric recombinant C-terminally His6-tagged enzyme, gel filtration Thermus thermophilus
1.3.5.1 120000
-
1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer Thermus thermophilus
1.3.5.1 120000
-
3 * 120000, about, wild-type enzyme, SDS-PAGE Thermus thermophilus
1.3.5.1 120000
-
4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex Thermus thermophilus
1.3.5.1 500000
-
wild-type enzyme, consisting of 360 kDa from protein and an unknown contribution of detergent and lipid, native PAGE Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 succinate + menaquinone Thermus thermophilus
-
fumarate + menaquinol
-
?
1.3.5.1 succinate + menaquinone Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
fumarate + menaquinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Thermus thermophilus
-
-
-
1.3.5.1 Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1 recombinant His6- or His8-tagged enzyme from Thermus thermophilus by nickel affinity chromatography and gel filtration, untagged enzyme by anion exchange chromatography and gel filtration Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 succinate + menaquinone
-
Thermus thermophilus fumarate + menaquinol
-
?
1.3.5.1 succinate + menaquinone
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 fumarate + menaquinol
-
?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 monomer 1 * 120000, about, recombinant C-terminally His6-tagged enzyme, SDS-PAGE, trimerization is disrupted in rcIISdhB-His6 due to the insertion of a hexahistidine tag on the C-terminus of SdhB subunit and the resulting protein complex can only form a monomer Thermus thermophilus
1.3.5.1 tetramer 4 * 120000, about, recombinant N-terminally His8-tagged enzyme, SDS-PAGE, four subunits of the rcII-His8-SdhB complex Thermus thermophilus
1.3.5.1 trimer 3 * 120000, about, wild-type enzyme, SDS-PAGE Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 SQR
-
Thermus thermophilus
1.3.5.1 succinate:quinone reductase
-
Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.5.1 30
-
assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.5.1 7.6
-
assay at Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 flavin covalently-bound flavin cofactor Thermus thermophilus
1.3.5.1 heme the enzyme contains two heme b cofactors, a di-heme Thermus thermophilus

General Information

EC Number General Information Comment Organism
1.3.5.1 physiological function succinate:quinone reductase serves as the respiratory complex II Thermus thermophilus