An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/59136 |
Resumo: | The bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemical sulfur cycle), the substrate- and quinone-binding sites of the QrcABCD complex are periplasmic, and their role in energy conservation has not been elucidated. Here we show that the QrcABCD complex of Desulfovibrio vulgaris is electrogenic, as protons and electrons required for quinone reduction are extracted from opposite sides of the membrane, with a H+/e− ratio of 1. Although the complex does not act as a H+-pump, QrcD may include a conserved proton channel leading from the N-side to the P-side menaquinone pocket. Our work provides evidence of how energy is conserved during dissimilatory sulfate reduction, and suggests mechanisms behind the functions of related bacterial respiratory complexes in other bioenergetic contexts. (...) |
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An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservationSulfatesDesulfovibrioThe bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemical sulfur cycle), the substrate- and quinone-binding sites of the QrcABCD complex are periplasmic, and their role in energy conservation has not been elucidated. Here we show that the QrcABCD complex of Desulfovibrio vulgaris is electrogenic, as protons and electrons required for quinone reduction are extracted from opposite sides of the membrane, with a H+/e− ratio of 1. Although the complex does not act as a H+-pump, QrcD may include a conserved proton channel leading from the N-side to the P-side menaquinone pocket. Our work provides evidence of how energy is conserved during dissimilatory sulfate reduction, and suggests mechanisms behind the functions of related bacterial respiratory complexes in other bioenergetic contexts. (...)Springer Nature [academic journals on nature.com]RUNG. Duarte, AméricoCatarino, TeresaWhite, Gaye F.Lousa, DianaNeukirchen, SinjeSoares, CláudioSousa, Filipa LClarke, Thomas A.Pereira, Inês A. C.2019-01-31T17:08:26Z2018-12-212018-12-21T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/59136eng20411723https://doi.org/10.1038/s41467-018-07839-xinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:28:28Zoai:run.unl.pt:10362/59136Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:33:21.488545Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
title |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
spellingShingle |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation G. Duarte, Américo Sulfates Desulfovibrio |
title_short |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
title_full |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
title_fullStr |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
title_full_unstemmed |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
title_sort |
An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation |
author |
G. Duarte, Américo |
author_facet |
G. Duarte, Américo Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio Sousa, Filipa L Clarke, Thomas A. Pereira, Inês A. C. |
author_role |
author |
author2 |
Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio Sousa, Filipa L Clarke, Thomas A. Pereira, Inês A. C. |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
RUN |
dc.contributor.author.fl_str_mv |
G. Duarte, Américo Catarino, Teresa White, Gaye F. Lousa, Diana Neukirchen, Sinje Soares, Cláudio Sousa, Filipa L Clarke, Thomas A. Pereira, Inês A. C. |
dc.subject.por.fl_str_mv |
Sulfates Desulfovibrio |
topic |
Sulfates Desulfovibrio |
description |
The bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemical sulfur cycle), the substrate- and quinone-binding sites of the QrcABCD complex are periplasmic, and their role in energy conservation has not been elucidated. Here we show that the QrcABCD complex of Desulfovibrio vulgaris is electrogenic, as protons and electrons required for quinone reduction are extracted from opposite sides of the membrane, with a H+/e− ratio of 1. Although the complex does not act as a H+-pump, QrcD may include a conserved proton channel leading from the N-side to the P-side menaquinone pocket. Our work provides evidence of how energy is conserved during dissimilatory sulfate reduction, and suggests mechanisms behind the functions of related bacterial respiratory complexes in other bioenergetic contexts. (...) |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12-21 2018-12-21T00:00:00Z 2019-01-31T17:08:26Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/59136 |
url |
http://hdl.handle.net/10362/59136 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
20411723 https://doi.org/10.1038/s41467-018-07839-x |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Springer Nature [academic journals on nature.com] |
publisher.none.fl_str_mv |
Springer Nature [academic journals on nature.com] |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137955198009344 |