Succinate dehydrogenase: Difference between revisions
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Succinate dehydrogenase, or mitochondrial respiratory Complex II or succinate:ubiquinone oxidoreductase (SQR) is an enzyme that catalyses the oxidation reaction between [[Succinate|succinate]] and [[ | Succinate dehydrogenase, or mitochondrial respiratory Complex II or succinate:ubiquinone oxidoreductase (SQR) is an enzyme that catalyses the oxidation reaction between [[Succinate|succinate]] and [[Fumarate|fumarate]] ([[FAD|FAD]] removes two [[Hydrogen|hydrogen]] atoms from succinate, resulting in a [[Double bond|double bond]] formation between the two [[Carbon|carbon]] atoms, giving the product fumarate)<ref>Alberts, Bruce. "2." Molecular Biology of the Cell. 5th ed. New York: Garland Science, 2008. 122-23. Print.</ref>. It has four subunits: two [[Hydrophilic|hydrophilic]] proteins ([[Flavoprotein|flavoprotein]] and iron-sulfur protein) and two [[Transmembrane proteins|transmembrane proteins]] (CybL and CybS)<ref>Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D et al. (2005). "Crystal structure of mitochondrial respiratory membrane protein complex II.". Cell 121 (7): 1043–57. doi:10.1016/j.cell.2005.05.025. PMID 15989954.</ref>.<br> | ||
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=== Reference === | === Reference === | ||
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Latest revision as of 13:57, 18 October 2015
Succinate dehydrogenase, or mitochondrial respiratory Complex II or succinate:ubiquinone oxidoreductase (SQR) is an enzyme that catalyses the oxidation reaction between succinate and fumarate (FAD removes two hydrogen atoms from succinate, resulting in a double bond formation between the two carbon atoms, giving the product fumarate)[1]. It has four subunits: two hydrophilic proteins (flavoprotein and iron-sulfur protein) and two transmembrane proteins (CybL and CybS)[2].
Reference
- ↑ Alberts, Bruce. "2." Molecular Biology of the Cell. 5th ed. New York: Garland Science, 2008. 122-23. Print.
- ↑ Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D et al. (2005). "Crystal structure of mitochondrial respiratory membrane protein complex II.". Cell 121 (7): 1043–57. doi:10.1016/j.cell.2005.05.025. PMID 15989954.