Succinate Dehydrogenase: Difference between revisions
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====Ubiquinone==== | ====Ubiquinone==== | ||
The binding site for ubiquinone, in which the substrate is reduced to ubiquinol, is bordered by subunits B, C, and D. Residues His207 of SdhB, Ser27 and Arg31 of SdhC, and Tyr83 of SdhD stabilize ubiquinone, while residues Pro160, Trp163, Trp164, and Ile209 of SdhB and Ser27 and Ile28 of SdhC provide the necessary hydrophobic environment that stabilizes the ring <ref>PMID:16407191</ref>. | The binding site for ubiquinone, in which the substrate is reduced to ubiquinol, is bordered by subunits B, C, and D. Residues His207 of SdhB, Ser27 and Arg31 of SdhC, and Tyr83 of SdhD stabilize ubiquinone, while residues Pro160, Trp163, Trp164, and Ile209 of SdhB and Ser27 and Ile28 of SdhC provide the necessary hydrophobic environment that stabilizes the ring <ref>PMID:16407191</ref>. | ||
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[[Image:S.D.Oxidation_of_Succinate_E2.gif]] | [[Image:S.D.Oxidation_of_Succinate_E2.gif]] | ||
Image 1: Oxidation of succinate to fumarate through E2 elimination | '''Image 1: Oxidation of succinate to fumarate through E2 elimination''' | ||
In the proposed E1cb mechanism, the deprotonation leads to the formation of an enolate intermediate; FAD then removes the hydride, as shown in Image 2 <ref>PMID:16950775</ref>. | In the proposed E1cb mechanism, the deprotonation leads to the formation of an enolate intermediate; FAD then removes the hydride, as shown in Image 2 <ref>PMID:16950775</ref>. | ||
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[[Image:S.D.Oxidation_of_Succinate_E1cb.gif]] | [[Image:S.D.Oxidation_of_Succinate_E1cb.gif]] | ||
Image 2: Oxidation of succinate to fumarate via E1cb elimination | '''Image 2: Oxidation of succinate to fumarate via E1cb elimination''' | ||
====Ubiquinone reduction==== | ====Ubiquinone reduction==== | ||
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[[Image:QuinoneMechanism.gif]] | [[Image:QuinoneMechanism.gif]] | ||
Image 3: Reduction of ubiquinone to ubiquinol | '''Image 3: Reduction of ubiquinone to ubiquinol''' | ||
===References:=== | ===References:=== | ||
<references/> | <references/> |