Electron-transfer pathways in the heme and quinone-binding domain of complex II (succinate dehydrogenase)

Robert F. Anderson, Sujata S. Shinde, Russ Hille, Richard A. Rothery, Joel H. Weiner, Sany Rajagukguk, Elena Maklashina, Gary Cecchini

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


Single electron transfers have been examined in complex II (succinate:ubiquinone oxidoreductase) by the method of pulse radiolysis. Electrons are introduced into the enzyme initially at the [3Fe-4S] and ubiquinone sites followed by intramolecular equilibration with the b heme of the enzyme. To define thermodynamic and other controlling parameters for the pathways of electron transfer in complex II, site-directed variants were constructed and analyzed. Variants at SdhB-His207 and SdhB-Ile209 exhibit significantly perturbed electron transfer between the [3Fe-4S] cluster and ubiquinone. Analysis of the data using Marcus theory shows that the electronic coupling constants for wild-type and variant enzyme are all small, indicating that electron transfer occurs by diabatic tunneling. The presence of the ubiquinone is necessary for efficient electron transfer to the heme, which only slowly equilibrates with the [3Fe-4S] cluster in the absence of the quinone.

Original languageEnglish
Pages (from-to)1637-1646
Number of pages10
Issue number10
Publication statusPublished - 1 Jan 2014
Externally publishedYes


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