Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | https://doi.org/10.1016/j.bbabio.2015.09.010 |
Resumo: | The authors thank Ricardo O. Louro for his helpful discussions. This work was supported by Fundacao para a Ciencia e Tecnologia (FCT) Portugal [Grants PTDC/QUI-BIQ/117440/2010, UID/Multi/04378/2013; APF and CMP were supported by FCT grants SFRH/BD/86439/2012 and SFRH/BPD/96952/2013, respectively]. The NMR spectrometers are part of The National NMR Facility, supported by FCT (RECI/BBB-BQB/0230/2012). |
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Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducensElectron transferExtracellular respirationGeobacterMultiheme cytochromesNanowiresBiophysicsBiochemistryCell BiologyThe authors thank Ricardo O. Louro for his helpful discussions. This work was supported by Fundacao para a Ciencia e Tecnologia (FCT) Portugal [Grants PTDC/QUI-BIQ/117440/2010, UID/Multi/04378/2013; APF and CMP were supported by FCT grants SFRH/BD/86439/2012 and SFRH/BPD/96952/2013, respectively]. The NMR spectrometers are part of The National NMR Facility, supported by FCT (RECI/BBB-BQB/0230/2012).The extracellular electron transfer metabolism of Geobacter sulfurreducens is sustained by several multiheme c-type cytochromes. One of these is the dodecaheme cytochrome GSU1996 that belongs to a new sub-class of c-type cytochromes. GSU1996 is composed by four similar triheme domains (A-D). The C-terminal half of the molecule encompasses the domains C and D, which are connected by a small linker and the N-terminal half of the protein contains two domains (A and B) that form one structural unit. It was proposed that this proteinworks as an electrically conductive device in G. sulfurreducens, transferring electrons within the periplasm or to outer-membrane cytochromes. In this work, a novel strategy was applied to characterize in detail the thermodynamic and kinetic properties of the hexaheme fragment CD of GSU1996. This characterization revealed the electron transfer process of GSU1996 for the first time, showing that a heme at the edge of the C-terminal of the protein is thermodynamic and kinetically competent to receive electrons from physiological redox partners. This information contributes towards understanding how this new sub-class of cytochromes functions as nanowires, and also increases the current knowledge of the extracellular electron transfer mechanisms in G. sulfurreducens.DQ - Departamento de QuímicaUCIBIO - Applied Molecular Biosciences UnitMolecular, Structural and Cellular Microbiology (MOSTMICRO)Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNAlves, Mónica N.Fernandes, Ana P.Salgueiro, Carlos A.Paquete, C.M.2018-05-03T22:04:40Z2016-01-012016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article7application/pdfhttps://doi.org/10.1016/j.bbabio.2015.09.010eng0005-2728PURE: 1581824http://www.scopus.com/inward/record.url?scp=84944929864&partnerID=8YFLogxKhttps://doi.org/10.1016/j.bbabio.2015.09.010info: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:RCAAP2024-03-11T04:19:31Zoai:run.unl.pt:10362/35897Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:30:22.861819Repositório 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 |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
title |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
spellingShingle |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens Alves, Mónica N. Electron transfer Extracellular respiration Geobacter Multiheme cytochromes Nanowires Biophysics Biochemistry Cell Biology |
title_short |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
title_full |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
title_fullStr |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
title_full_unstemmed |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
title_sort |
Unraveling the electron transfer processes of a nanowire protein from Geobacter sulfurreducens |
author |
Alves, Mónica N. |
author_facet |
Alves, Mónica N. Fernandes, Ana P. Salgueiro, Carlos A. Paquete, C.M. |
author_role |
author |
author2 |
Fernandes, Ana P. Salgueiro, Carlos A. Paquete, C.M. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
DQ - Departamento de Química UCIBIO - Applied Molecular Biosciences Unit Molecular, Structural and Cellular Microbiology (MOSTMICRO) Instituto de Tecnologia Química e Biológica António Xavier (ITQB) RUN |
dc.contributor.author.fl_str_mv |
Alves, Mónica N. Fernandes, Ana P. Salgueiro, Carlos A. Paquete, C.M. |
dc.subject.por.fl_str_mv |
Electron transfer Extracellular respiration Geobacter Multiheme cytochromes Nanowires Biophysics Biochemistry Cell Biology |
topic |
Electron transfer Extracellular respiration Geobacter Multiheme cytochromes Nanowires Biophysics Biochemistry Cell Biology |
description |
The authors thank Ricardo O. Louro for his helpful discussions. This work was supported by Fundacao para a Ciencia e Tecnologia (FCT) Portugal [Grants PTDC/QUI-BIQ/117440/2010, UID/Multi/04378/2013; APF and CMP were supported by FCT grants SFRH/BD/86439/2012 and SFRH/BPD/96952/2013, respectively]. The NMR spectrometers are part of The National NMR Facility, supported by FCT (RECI/BBB-BQB/0230/2012). |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-01-01 2016-01-01T00:00:00Z 2018-05-03T22:04:40Z |
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 |
https://doi.org/10.1016/j.bbabio.2015.09.010 |
url |
https://doi.org/10.1016/j.bbabio.2015.09.010 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0005-2728 PURE: 1581824 http://www.scopus.com/inward/record.url?scp=84944929864&partnerID=8YFLogxK https://doi.org/10.1016/j.bbabio.2015.09.010 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
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openAccess |
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7 application/pdf |
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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 |
reponame_str |
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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