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Literature summary extracted from

  • Fernandes, A.S.; Pereira, M.M.; Teixeira, M.
    The succinate dehydrogenase from the thermohalophilic bacterium Rhodothermus marinus: Redox-Bohr effect on heme bL (2001), J. Bioenerg. Biomembr., 33, 343-352.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.1 0.1
-
 fumarate 65°C, pH 6.5 Rhodothermus marinus
1.3.5.1 0.165
-
 succinate 65°C, pH 6.5 Rhodothermus marinus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.5.1 18000
-
 1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE Rhodothermus marinus
1.3.5.1 32000
-
 1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE Rhodothermus marinus
1.3.5.1 70000
-
 1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE Rhodothermus marinus

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Rhodothermus marinus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 fumarate + reduced benzyl viologen
-
 Rhodothermus marinus succinate + benzyl viologen
-
 ?
1.3.5.1 succinate + benzyl viologen
-
 Rhodothermus marinus fumarate + reduced benzyl viologen
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 ? 1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE Rhodothermus marinus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.5.1 80
-
-
 Rhodothermus marinus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.5.1 79.6
-
 fumarate 65°C, pH 6.5 Rhodothermus marinus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 heme
-
 Rhodothermus marinus
1.3.5.1 iron-sulfur centre enzyme contains the canonical iron-sulfur centers S1, S2, and S3, as well as two B-type hemes. The S3 center has a high reduction potential of +130 mV and is present in two different conformations, one of which presents an EPR signal with g values at 2.035, 2.009, and 2.001. The apparent midpoint reduction potentials of the hemes, +75 and -65 mV at pH 7.5, are higher than those reported for other enzymes. The heme with the lower potential, heme bL, presents a considerable dependence of the reduction potential with pH, i.e. a redox-Bohr effect, having a pKox of 6.5 and a pKred of 8.7. This behavior is consistent with the proposal that in these enzymes menaquinone reduction occurs close to heme bL, near to the periplasmic side of the membrane, and involving dissipation of the proton transmembrane gradient Rhodothermus marinus