Crystallization (Comment) | Organism |
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three new structures of Escherichia coli succinate-quinone oxidoreductase are solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present is solved at 2.4 A resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. Comparison of the new succinate-quinone oxidoreductase structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
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carboxin | - |
Escherichia coli | |
Pentachlorophenol | - |
Escherichia coli |
Organism | UniProt | Comment | Textmining |
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Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate + oxidized 2,6-dichlorophenolindophenol | in the presence of the artificial electron acceptor phenazine methosulfate and the ubiquinone analogue UQ1 | Escherichia coli | fumarate + reduced 2,6-dichloroindophenol | - |
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Synonyms | Comment | Organism |
---|---|---|
SQR | - |
Escherichia coli |
succinate-quinone oxidoreductase | - |
Escherichia coli |