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Succinate - coenzyme Q reductase
Succinate-coenzyme Q reductase (EC 22.214.171.124 ; succinate dehydrogenase) is an enzyme complex bound to the inner mitochondrial membrane. It is the only enzyme that participates in both the citric acid cycle and the mitochondrial electron transport chain (in this role it is often called Complex II). It is the only citric acid cycle enzyme that is membrane-bound. It is found in many aerobic and anaerobic organisms including Escherichia coli. The enzyme complex is a heterotetramer divided into three domains: SDHA, the catalytic domain; SDHB, the electron transfer subunit; SDHC/SDHD, the dimeric membrane anchor that contains β -type heme.
Additional recommended knowledge
Function of the Succinate-coenzyme Q Reductase Complex
The function of the enzyme is illustrated by following the transfer of electrons from succinate to ubiquinol. The electron path is shown in the diagram by the red arrows.
Role in Disease
The fundamental role of succinate-coenzyme Q reductase in the electron transfer chain of mitochondria makes it vital in most multicellular organisms, removal of this enzyme from the genome has also been shown to be lethal at the embryonic stage in mice.
SDHB, SDHC and SDHD exhibit classic tumor suppressor gene behavior. SDHA has never been reported to be a tumor suppressor. The resulting disease depends on which gene is mutated.
The precise mechanism for each of these disease pathways is still being determined. See the specific gene for more details. Other diseases linked to succinate dehydrogenase include hereditary paraganglioma, obsessive compulsive disorder, generation of aromatic flatulants, and dwarfism.
Categories: Cellular respiration | Iron-sulfur proteins | Integral membrane proteins
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Succinate_-_coenzyme_Q_reductase". A list of authors is available in Wikipedia.|