Succinate Dehydrogenase: Difference between revisions
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{{STRUCTURE_2wdv| PDB=2wdv | SIZE=400| SCENE= |right|CAPTION=Succinate dehydrogenase complex with FAD, protoporphrin, malate, Na+ ion, Fe2S2, Fe3S4, Fe4S4, [[2wdv]] }} | |||
[[Succinate Dehydrogenase]] (PDB = [[2wdv]] with empty ubiquinone binding site; PDB = [[1nek]] with ubiquinone bound), also called succinate-coenzyme Q reductase (SQR) or Complex II, is a tetrameric enzyme found in the cell membrane of some bacteria and the inner mitochondrial membrane of mammalian cells. It is classified as an α+β protein, as it contains <scene name='Michael_Vick_Sandbox_2/2wdv_sec_structure/1'>segregated regions</scene> of α helices and antiparallel β sheets. It is involved in two aspects of digestion; it catalyzes the oxidation of succinate to fumarate in the citric acid cycle by simultaneously reducing ubiquinone to ubiquinol in the electron transport chain <ref>PMID:14672929</ref>. | [[Succinate Dehydrogenase]] (PDB = [[2wdv]] with empty ubiquinone binding site; PDB = [[1nek]] with ubiquinone bound), also called succinate-coenzyme Q reductase (SQR) or Complex II, is a tetrameric enzyme found in the cell membrane of some bacteria and the inner mitochondrial membrane of mammalian cells. It is classified as an α+β protein, as it contains <scene name='Michael_Vick_Sandbox_2/2wdv_sec_structure/1'>segregated regions</scene> of α helices and antiparallel β sheets. It is involved in two aspects of digestion; it catalyzes the oxidation of succinate to fumarate in the citric acid cycle by simultaneously reducing ubiquinone to ubiquinol in the electron transport chain <ref>PMID:14672929</ref>. | ||