Literature summary for 1.3.5.1 extracted from

Ruprecht, J.; Yankovskaya, V.; Maklashina, E.; Iwata, S.; Cecchini, G.
Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site (2009), J. Biol. Chem., 284, 29836-29846.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Inhibitors	Comment	Organism	Structure
carboxin	-	Escherichia coli
Pentachlorophenol	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

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	-	?

Synonyms

Synonyms	Comment	Organism
SQR	-	Escherichia coli
succinate-quinone oxidoreductase	-	Escherichia coli

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Release 2023.1 (January 2023)