Literature summary for 1.3.5.1 extracted from

Silkin, Y.; Oyedotun, K.S.; Lemire, B.D.
The role of Sdh4p Tyr-89 in ubiquinone reduction by the Saccharomyces cerevisiae succinate dehydrogenase (2006), Biochim. Biophys. Acta, 1767, 143-150.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	bound	Saccharomyces cerevisiae	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe-S cluster	two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
succinate + ubiquinone	two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol, role of Tyr-89 in the protonation of ubiquinone	Saccharomyces cerevisiae	fumarate + ubiquinol	-	?

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Release 2023.1 (January 2023)