Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus

Detalhes bibliográficos
Autor(a) principal: Guerra, João P.L.
Data de Publicação: 2023
Outros Autores: Penas, Daniela, Tavares, Pedro, Pereira, Alice S.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/158334
Resumo: Funding Information: This work was financed by national funds from the Fundação para a Ciência e a Tecnologia (FCT-MCTES), I.P., in the scope of the project UIDB/04378/2020 of the Research Unit on Applied Molecular Biosciences–UCIBIO and LA/P/0140/2020 of the Associate Laboratory Institute for Health and Bioeconomy–i4HB; grant PTDC/BIAPRO/111485/2009 (to P.T.) and PTDC/QUI/64248/2006 (to A.S.P). This work was also supported by the Radiation Biology and Biophysics Doctoral Training Program–RaBBiT, financed by FCT-MCTES, grants PD/00193/2012; UIDB/04378/2020 (UCIBIO) and UIDB/00068/2020 (CEFITEC). The RaBBiT Doctoral Training Program awarded fellowships to J.P.L.G. (PD/BD/135476/2017 and COVID/BD/152497/2022) and to D.P. (SFRH/BD/52535/2014). Publisher Copyright: © 2023 by the authors.
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spelling Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticuscopper in biologyDNA-binding protein from starved cells (Dps)electron paramagnetic resonance spectroscopy (EPR)ferroxidase centersiron homeostasisiron oxidationMössbauer spectroscopytransition metals in biologyCatalysisMolecular BiologySpectroscopyComputer Science ApplicationsPhysical and Theoretical ChemistryOrganic ChemistryInorganic ChemistrySDG 14 - Life Below WaterFunding Information: This work was financed by national funds from the Fundação para a Ciência e a Tecnologia (FCT-MCTES), I.P., in the scope of the project UIDB/04378/2020 of the Research Unit on Applied Molecular Biosciences–UCIBIO and LA/P/0140/2020 of the Associate Laboratory Institute for Health and Bioeconomy–i4HB; grant PTDC/BIAPRO/111485/2009 (to P.T.) and PTDC/QUI/64248/2006 (to A.S.P). This work was also supported by the Radiation Biology and Biophysics Doctoral Training Program–RaBBiT, financed by FCT-MCTES, grants PD/00193/2012; UIDB/04378/2020 (UCIBIO) and UIDB/00068/2020 (CEFITEC). The RaBBiT Doctoral Training Program awarded fellowships to J.P.L.G. (PD/BD/135476/2017 and COVID/BD/152497/2022) and to D.P. (SFRH/BD/52535/2014). Publisher Copyright: © 2023 by the authors.Dps proteins (DNA-binding proteins from starved cells) are multifunctional stress defense proteins from the Ferritin family expressed in Prokarya during starvation and/or acute oxidative stress. Besides shielding bacterial DNA through binding and condensation, Dps proteins protect the cell from reactive oxygen species by oxidizing and storing ferrous ions within their cavity, using either hydrogen peroxide or molecular oxygen as the co-substrate, thus reducing the toxic effects of Fenton reactions. Interestingly, the interaction between Dps and transition metals (other than iron) is a known but relatively uncharacterized phenomenon. The impact of non-iron metals on the structure and function of Dps proteins is a current topic of research. This work focuses on the interaction between the Dps from Marinobacter nauticus (a marine facultative anaerobe bacterium capable of degrading petroleum hydrocarbons) and the cupric ion (Cu2+), one of the transition metals of greater biological relevance. Results obtained using electron paramagnetic resonance (EPR), Mössbauer and UV/Visible spectroscopies revealed that Cu2+ ions bind to specific binding sites in Dps, exerting a rate-enhancing effect on the ferroxidation reaction in the presence of molecular oxygen and directly oxidizing ferrous ions when no other co-substrate is present, in a yet uncharacterized redox reaction. This prompts additional research on the catalytic properties of Dps proteins.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNGuerra, João P.L.Penas, DanielaTavares, PedroPereira, Alice S.2023-09-26T22:21:33Z2023-062023-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article14application/pdfhttp://hdl.handle.net/10362/158334eng1661-6596PURE: 72481539https://doi.org/10.3390/ijms241210256info: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:RCAAP2024-03-11T05:40:40Zoai:run.unl.pt:10362/158334Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:57:04.916282Repositório 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 Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
title Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
spellingShingle Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
Guerra, João P.L.
copper in biology
DNA-binding protein from starved cells (Dps)
electron paramagnetic resonance spectroscopy (EPR)
ferroxidase centers
iron homeostasis
iron oxidation
Mössbauer spectroscopy
transition metals in biology
Catalysis
Molecular Biology
Spectroscopy
Computer Science Applications
Physical and Theoretical Chemistry
Organic Chemistry
Inorganic Chemistry
SDG 14 - Life Below Water
title_short Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
title_full Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
title_fullStr Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
title_full_unstemmed Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
title_sort Influence of Cupric (Cu2+) Ions on the Iron Oxidation Mechanism by DNA-Binding Protein from Starved Cells (Dps) from Marinobacter nauticus
author Guerra, João P.L.
author_facet Guerra, João P.L.
Penas, Daniela
Tavares, Pedro
Pereira, Alice S.
author_role author
author2 Penas, Daniela
Tavares, Pedro
Pereira, Alice S.
author2_role author
author
author
dc.contributor.none.fl_str_mv UCIBIO - Applied Molecular Biosciences Unit
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Guerra, João P.L.
Penas, Daniela
Tavares, Pedro
Pereira, Alice S.
dc.subject.por.fl_str_mv copper in biology
DNA-binding protein from starved cells (Dps)
electron paramagnetic resonance spectroscopy (EPR)
ferroxidase centers
iron homeostasis
iron oxidation
Mössbauer spectroscopy
transition metals in biology
Catalysis
Molecular Biology
Spectroscopy
Computer Science Applications
Physical and Theoretical Chemistry
Organic Chemistry
Inorganic Chemistry
SDG 14 - Life Below Water
topic copper in biology
DNA-binding protein from starved cells (Dps)
electron paramagnetic resonance spectroscopy (EPR)
ferroxidase centers
iron homeostasis
iron oxidation
Mössbauer spectroscopy
transition metals in biology
Catalysis
Molecular Biology
Spectroscopy
Computer Science Applications
Physical and Theoretical Chemistry
Organic Chemistry
Inorganic Chemistry
SDG 14 - Life Below Water
description Funding Information: This work was financed by national funds from the Fundação para a Ciência e a Tecnologia (FCT-MCTES), I.P., in the scope of the project UIDB/04378/2020 of the Research Unit on Applied Molecular Biosciences–UCIBIO and LA/P/0140/2020 of the Associate Laboratory Institute for Health and Bioeconomy–i4HB; grant PTDC/BIAPRO/111485/2009 (to P.T.) and PTDC/QUI/64248/2006 (to A.S.P). This work was also supported by the Radiation Biology and Biophysics Doctoral Training Program–RaBBiT, financed by FCT-MCTES, grants PD/00193/2012; UIDB/04378/2020 (UCIBIO) and UIDB/00068/2020 (CEFITEC). The RaBBiT Doctoral Training Program awarded fellowships to J.P.L.G. (PD/BD/135476/2017 and COVID/BD/152497/2022) and to D.P. (SFRH/BD/52535/2014). Publisher Copyright: © 2023 by the authors.
publishDate 2023
dc.date.none.fl_str_mv 2023-09-26T22:21:33Z
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/10362/158334
url http://hdl.handle.net/10362/158334
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1661-6596
PURE: 72481539
https://doi.org/10.3390/ijms241210256
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 14
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
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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