Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
Autor(a) principal: | |
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Data de Publicação: | 2023 |
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/10362/158558 |
Resumo: | Funding Information: Financial support was provided by the European EC Horizon2020 TIMB3 (Project 810856) and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska Curie ITN ConCO2rde (grant agreement No 955740), as well as the COST Action CA21115 Iron–sulphur (FeS) clusters: from chemistry to immunology (FeSImmChemNet). This work was funded by national funds through FC—Fundação para a Ciência e a Tecnologia, I.P. (FCT), Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and the LS4FUTURE Associated Laboratory (LA/P/0087/2020). The N-terminal sequencing service was provided by the ITQB Research facilities. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by the FCT, project AAC 01/SAICT/2016. The IBT was financially supported by national funds through the FCT PT-NMR PhD Program via PD/BD/135187/2017. This work benefited of the support and the use of resources of Instruct-ERIC, specifically the CERM/CIRMMP Italy Centre (PID 4509). Publisher Copyright: © 2023 by the authors. |
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Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidationbiological electron transfercytochrome cHIPIPparamagnetic NMRphotoferrotrophismprotein interactionsRhodopseudomonasAnalytical ChemistryChemistry (miscellaneous)Molecular MedicinePharmaceutical ScienceDrug DiscoveryPhysical and Theoretical ChemistryOrganic ChemistryFunding Information: Financial support was provided by the European EC Horizon2020 TIMB3 (Project 810856) and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska Curie ITN ConCO2rde (grant agreement No 955740), as well as the COST Action CA21115 Iron–sulphur (FeS) clusters: from chemistry to immunology (FeSImmChemNet). This work was funded by national funds through FC—Fundação para a Ciência e a Tecnologia, I.P. (FCT), Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and the LS4FUTURE Associated Laboratory (LA/P/0087/2020). The N-terminal sequencing service was provided by the ITQB Research facilities. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by the FCT, project AAC 01/SAICT/2016. The IBT was financially supported by national funds through the FCT PT-NMR PhD Program via PD/BD/135187/2017. This work benefited of the support and the use of resources of Instruct-ERIC, specifically the CERM/CIRMMP Italy Centre (PID 4509). Publisher Copyright: © 2023 by the authors.Rhodopseudomonas palustris is an alphaproteobacterium with impressive metabolic versatility, capable of oxidizing ferrous iron to fix carbon dioxide using light energy. Photoferrotrophic iron oxidation is one of the most ancient metabolisms, sustained by the pio operon coding for three proteins: PioB and PioA, which form an outer-membrane porin–cytochrome complex that oxidizes iron outside of the cell and transfers the electrons to the periplasmic high potential iron–sulfur protein (HIPIP) PioC, which delivers them to the light-harvesting reaction center (LH-RC). Previous studies have shown that PioA deletion is the most detrimental for iron oxidation, while, the deletion of PioC resulted in only a partial loss. The expression of another periplasmic HiPIP, designated Rpal_4085, is strongly upregulated in photoferrotrophic conditions, making it a strong candidate for a PioC substitute. However, it is unable to reduce the LH-RC. In this work we used NMR spectroscopy to map the interactions between PioC, PioA, and the LH-RC, identifying the key amino acid residues involved. We also observed that PioA directly reduces the LH-RC, and this is the most likely substitute upon PioC deletion. By contrast, Rpal_4085 demontrated significant electronic and structural differences from PioC. These differences likely explain its inability to reduce the LH-RC and highlight its distinct functional role. Overall, this work reveals the functional resilience of the pio operon pathway and further highlights the use of paramagnetic NMR for understanding key biological processes.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNTrindade, Inês B.Firmino, Maria O.Noordam, Sander J.Alves, Alexandra S.Fonseca, Bruno M.Piccioli, MarioLouro, Ricardo O.2023-09-30T22:23:03Z2023-062023-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/158558eng1420-3049PURE: 72787972https://doi.org/10.3390/molecules28124733info: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:RCAAP2024-05-22T18:14:52Zoai:run.unl.pt:10362/158558Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T18:14:52Repositório 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 |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
title |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
spellingShingle |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation Trindade, Inês B. biological electron transfer cytochrome c HIPIP paramagnetic NMR photoferrotrophism protein interactions Rhodopseudomonas Analytical Chemistry Chemistry (miscellaneous) Molecular Medicine Pharmaceutical Science Drug Discovery Physical and Theoretical Chemistry Organic Chemistry |
title_short |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
title_full |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
title_fullStr |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
title_full_unstemmed |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
title_sort |
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation |
author |
Trindade, Inês B. |
author_facet |
Trindade, Inês B. Firmino, Maria O. Noordam, Sander J. Alves, Alexandra S. Fonseca, Bruno M. Piccioli, Mario Louro, Ricardo O. |
author_role |
author |
author2 |
Firmino, Maria O. Noordam, Sander J. Alves, Alexandra S. Fonseca, Bruno M. Piccioli, Mario Louro, Ricardo O. |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Instituto de Tecnologia Química e Biológica António Xavier (ITQB) RUN |
dc.contributor.author.fl_str_mv |
Trindade, Inês B. Firmino, Maria O. Noordam, Sander J. Alves, Alexandra S. Fonseca, Bruno M. Piccioli, Mario Louro, Ricardo O. |
dc.subject.por.fl_str_mv |
biological electron transfer cytochrome c HIPIP paramagnetic NMR photoferrotrophism protein interactions Rhodopseudomonas Analytical Chemistry Chemistry (miscellaneous) Molecular Medicine Pharmaceutical Science Drug Discovery Physical and Theoretical Chemistry Organic Chemistry |
topic |
biological electron transfer cytochrome c HIPIP paramagnetic NMR photoferrotrophism protein interactions Rhodopseudomonas Analytical Chemistry Chemistry (miscellaneous) Molecular Medicine Pharmaceutical Science Drug Discovery Physical and Theoretical Chemistry Organic Chemistry |
description |
Funding Information: Financial support was provided by the European EC Horizon2020 TIMB3 (Project 810856) and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska Curie ITN ConCO2rde (grant agreement No 955740), as well as the COST Action CA21115 Iron–sulphur (FeS) clusters: from chemistry to immunology (FeSImmChemNet). This work was funded by national funds through FC—Fundação para a Ciência e a Tecnologia, I.P. (FCT), Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and the LS4FUTURE Associated Laboratory (LA/P/0087/2020). The N-terminal sequencing service was provided by the ITQB Research facilities. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by the FCT, project AAC 01/SAICT/2016. The IBT was financially supported by national funds through the FCT PT-NMR PhD Program via PD/BD/135187/2017. This work benefited of the support and the use of resources of Instruct-ERIC, specifically the CERM/CIRMMP Italy Centre (PID 4509). Publisher Copyright: © 2023 by the authors. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-09-30T22:23:03Z 2023-06 2023-06-01T00:00:00Z |
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/10362/158558 |
url |
http://hdl.handle.net/10362/158558 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1420-3049 PURE: 72787972 https://doi.org/10.3390/molecules28124733 |
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.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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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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mluisa.alvim@gmail.com |
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