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Literature summary extracted from

  • Horsefield, R.; Yankovskaya, V.; Sexton, G.; Whittingham, W.; Shiomi, K.; Omura, S.; Byrne, B.; Cecchini, G.; Iwata, S.
    Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction (2006), J. Biol. Chem., 281, 7309-7316.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.5.1 hanging-drop vapour-diffusion method, the enzyme is cocrystallized with the ubiquinone binding-site inhibitor Atpenin A5 (AA5) to confirm the binding position of the inhibitor and reveal additional structural details of the Q-site Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 atpenin 5A
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 succinate + ubiquinone Escherichia coli succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol fumarate + ubiquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 succinate + ubiquinone succinate dehydrogenase is a functional member of the Krebs cycle and the aerobic respiratory chain and couples the oxidation of succinate to fumarate with the reduction of quinone to quinol Escherichia coli fumarate + ubiquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 complex II
-
 Escherichia coli
1.3.5.1 succinate-ubiquinone oxidoreductase
-
 Escherichia coli