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Literature summary for 1.3.5.1 extracted from
- Succinate: quinone oxidoreductases - what can we learn from Wolinella succinogenes quinol:fumarate reductase? (2001), FEBS Lett., 504, 133-141.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| fumarate reductase, determined at 3.3 A, belongs to the type D enzymes: contains two hydrophobic subunits and no heme group | Escherichia coli |
| fumarate reductase, refined at 2.2-A resolution, belongs to the type B enzymes: contains one hydrophobic subunit and two heme groups | Wolinella succinogenes |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 27000 | - |
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer | Wolinella succinogenes |
| 30000 | - |
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer | Wolinella succinogenes |
| 73000 | - |
1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer | Wolinella succinogenes |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Wolinella succinogenes | succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate | ? | - |
? |  |
| succinate + ubiquinone | Escherichia coli | - |
fumarate + ubiquinol | - |
r | |
| succinate + ubiquinone | Wolinella succinogenes | - |
fumarate + ubiquinol | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
fumarate reductase | - |
| Wolinella succinogenes | - |
succinate dehydrogenase | - |
| Wolinella succinogenes | - |
formerly Vibrio succinogenes, fumarate reductase | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| fumarate + quinol | - |
Escherichia coli | succinate + ubiquinone | - |
r | |
| fumarate + quinol | - |
Wolinella succinogenes | succinate + ubiquinone | - |
r | |
| additional information | succinate dehydrogenase is involved in aerobic metabolism as part of the citric acid cycle and of the aerobic respiratory chain, fumarate reductase participates in anaerobic respiration with fumarate as the terminal electron acceptor and is part of the electron transport chain catalysing the oxidation of various donor substrates by fumarate | Wolinella succinogenes | ? | - |
? | |
| succinate + ubiquinone | - |
Escherichia coli | fumarate + ubiquinol | - |
r | |
| succinate + ubiquinone | - |
Wolinella succinogenes | fumarate + ubiquinol | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| trimer | 1 * 73000 + 1 * 27000 + 1 * 30000, three structures of the enzyme based on three different crystal forms are available, in all three crystal forms two heterotrimeric complexes of A,B and C subunits are associated in an identical fashion, forming a dimer | Wolinella succinogenes |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome b | - |
Escherichia coli | |
| cytochrome b | - |
Wolinella succinogenes | |
| FAD | covalently bound to flavoprotein subunit | Escherichia coli | |
| FAD | covalently bound to flavoprotein subunit | Wolinella succinogenes | |
| additional information | the enzyme contains iron-sulfur centers | Escherichia coli | |
| additional information | the enzyme contains iron-sulfur centers | Wolinella succinogenes |
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