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Literature summary for 1.3.5.1 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]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Rhodothermus marinus
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
heme
-
Rhodothermus marinus
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