Succinate dehydrogenase

The printable version is no longer supported and may have rendering errors. Please update your browser bookmarks and please use the default browser print function instead.

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 fumerate)^[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.

[1] Alberts, Bruce. "2." Molecular Biology of the Cell. 5th ed. New York: Garland Science, 2008. 122-23. Print.

[2] 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.

[1]

[2]

Succinate dehydrogenase

Reference

Navigation menu

Search