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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Rhodothermus marinus | - |
- |
- |
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 | Comment | Organism |
---|---|---|
? | 1 * 70000, flavoprotein, + 1 * 32000, iron-sulfur protein, + 1 * 18000, SDS-PAGE | Rhodothermus marinus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
- |
Rhodothermus marinus |
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 | 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 |