An electrogenic redox loop in sulfate reductionreveals a likely widespread mechanism of energy conservation

Detalhes bibliográficos
Autor(a) principal: G. Duarte, Américo
Data de Publicação: 2018
Outros Autores: Catarino, Teresa, White, Gaye F., Lousa, Diana, Neukirchen, Sinje, Soares, Cláudio, Sousa, Filipa L, Clarke, Thomas A., Pereira, Inês A. C.
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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spelling 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
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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