Electron-transfer chain in respiratory complex I

Abstract Complex I is a part of the respiration energy chain converting the redox energy into the cross-membrane proton gradient. The electron-transfer chain of iron-sulfur cofactors within the water-soluble peripheral part of the complex is responsible for the delivery of electrons to the proton pu...

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Autores principales:	Daniel R. Martin, Dmitry V. Matyushov
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6174f3f440204064b48e587c29e5cbca
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spelling	oai:doaj.org-article:6174f3f440204064b48e587c29e5cbca2021-12-02T11:40:22ZElectron-transfer chain in respiratory complex I10.1038/s41598-017-05779-y2045-2322https://doaj.org/article/6174f3f440204064b48e587c29e5cbca2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05779-yhttps://doaj.org/toc/2045-2322Abstract Complex I is a part of the respiration energy chain converting the redox energy into the cross-membrane proton gradient. The electron-transfer chain of iron-sulfur cofactors within the water-soluble peripheral part of the complex is responsible for the delivery of electrons to the proton pumping subunit. The protein is porous to water penetration and the hydration level of the cofactors changes when the electron is transferred along the chain. High reaction barriers and trapping of the electrons at the iron-sulfur cofactors are prevented by the combination of intense electrostatic noise produced by the protein-water interface with the high density of quantum states in the iron-sulfur clusters caused by spin interactions between paramagnetic iron atoms. The combination of these factors substantially lowers the activation barrier for electron transfer compared to the prediction of the Marcus theory, bringing the rate to the experimentally established range. The unique role of iron-sulfur clusters as electron-transfer cofactors is in merging protein-water fluctuations with quantum-state multiplicity to allow low activation barriers and robust operation. Water plays a vital role in electron transport energetics by electrowetting the cofactors in the chain upon arrival of the electron. A general property of a protein is to violate the fluctuation-dissipation relation through nonergodic sampling of its landscape. High functional efficiency of redox enzymes is a direct consequence of nonergodicity.Daniel R. MartinDmitry V. MatyushovNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Daniel R. Martin Dmitry V. Matyushov Electron-transfer chain in respiratory complex I
description	Abstract Complex I is a part of the respiration energy chain converting the redox energy into the cross-membrane proton gradient. The electron-transfer chain of iron-sulfur cofactors within the water-soluble peripheral part of the complex is responsible for the delivery of electrons to the proton pumping subunit. The protein is porous to water penetration and the hydration level of the cofactors changes when the electron is transferred along the chain. High reaction barriers and trapping of the electrons at the iron-sulfur cofactors are prevented by the combination of intense electrostatic noise produced by the protein-water interface with the high density of quantum states in the iron-sulfur clusters caused by spin interactions between paramagnetic iron atoms. The combination of these factors substantially lowers the activation barrier for electron transfer compared to the prediction of the Marcus theory, bringing the rate to the experimentally established range. The unique role of iron-sulfur clusters as electron-transfer cofactors is in merging protein-water fluctuations with quantum-state multiplicity to allow low activation barriers and robust operation. Water plays a vital role in electron transport energetics by electrowetting the cofactors in the chain upon arrival of the electron. A general property of a protein is to violate the fluctuation-dissipation relation through nonergodic sampling of its landscape. High functional efficiency of redox enzymes is a direct consequence of nonergodicity.
format	article
author	Daniel R. Martin Dmitry V. Matyushov
author_facet	Daniel R. Martin Dmitry V. Matyushov
author_sort	Daniel R. Martin
title	Electron-transfer chain in respiratory complex I
title_short	Electron-transfer chain in respiratory complex I
title_full	Electron-transfer chain in respiratory complex I
title_fullStr	Electron-transfer chain in respiratory complex I
title_full_unstemmed	Electron-transfer chain in respiratory complex I
title_sort	electron-transfer chain in respiratory complex i
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6174f3f440204064b48e587c29e5cbca
work_keys_str_mv	AT danielrmartin electrontransferchaininrespiratorycomplexi AT dmitryvmatyushov electrontransferchaininrespiratorycomplexi
_version_	1718395645589454848

Electron-transfer chain in respiratory complex I

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