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Electron-Transfer Pathways in the Heme and Quinone-Binding Domain of Complex II (Succinate Dehydrogenase)
[Image: see text] 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 th...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985935/ https://www.ncbi.nlm.nih.gov/pubmed/24559074 http://dx.doi.org/10.1021/bi401630m |
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author | Anderson, Robert F. Shinde, Sujata S. Hille, Russ Rothery, Richard A. Weiner, Joel H. Rajagukguk, Sany Maklashina, Elena Cecchini, Gary |
author_facet | Anderson, Robert F. Shinde, Sujata S. Hille, Russ Rothery, Richard A. Weiner, Joel H. Rajagukguk, Sany Maklashina, Elena Cecchini, Gary |
author_sort | Anderson, Robert F. |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-3985935 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-39859352015-02-21 Electron-Transfer Pathways in the Heme and Quinone-Binding Domain of Complex II (Succinate Dehydrogenase) Anderson, Robert F. Shinde, Sujata S. Hille, Russ Rothery, Richard A. Weiner, Joel H. Rajagukguk, Sany Maklashina, Elena Cecchini, Gary Biochemistry [Image: see text] 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. American Chemical Society 2014-02-21 2014-03-18 /pmc/articles/PMC3985935/ /pubmed/24559074 http://dx.doi.org/10.1021/bi401630m Text en Copyright © 2014 American Chemical Society |
spellingShingle | Anderson, Robert F. Shinde, Sujata S. Hille, Russ Rothery, Richard A. Weiner, Joel H. Rajagukguk, Sany Maklashina, Elena Cecchini, Gary Electron-Transfer Pathways in the Heme and Quinone-Binding Domain of Complex II (Succinate Dehydrogenase) |
title | Electron-Transfer Pathways in the Heme and Quinone-Binding
Domain of Complex II (Succinate Dehydrogenase) |
title_full | Electron-Transfer Pathways in the Heme and Quinone-Binding
Domain of Complex II (Succinate Dehydrogenase) |
title_fullStr | Electron-Transfer Pathways in the Heme and Quinone-Binding
Domain of Complex II (Succinate Dehydrogenase) |
title_full_unstemmed | Electron-Transfer Pathways in the Heme and Quinone-Binding
Domain of Complex II (Succinate Dehydrogenase) |
title_short | Electron-Transfer Pathways in the Heme and Quinone-Binding
Domain of Complex II (Succinate Dehydrogenase) |
title_sort | electron-transfer pathways in the heme and quinone-binding
domain of complex ii (succinate dehydrogenase) |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985935/ https://www.ncbi.nlm.nih.gov/pubmed/24559074 http://dx.doi.org/10.1021/bi401630m |
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