Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens

Detalhes bibliográficos
Autor(a) principal: Teixeira, Liliana R.
Data de Publicação: 2020
Outros Autores: Cordas, Cristina M., Fonseca, Marta P., Duke, Norma E. C., Pokkuluri, Phani Raj, Salgueiro, Carlos A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/117015
Resumo: PD/00193/2012 UID/FIS/00068/2019 PTDC/BBBBQB/3554/2014 PTDC/BIA-BQM/31981/2017 PD/BD/114445/2016 UID/Multi/04378/2019 ROTEIRO/0031/2013 -PINFRA/22161/2016
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spelling Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducensc-type cytochromecyclic voltammetryelectron transfer proteinsnuclear magnetic resonanceredox-Bohr effectsite-directed mutagenesisX-ray crystallographyMicrobiologyMicrobiology (medical)PD/00193/2012 UID/FIS/00068/2019 PTDC/BBBBQB/3554/2014 PTDC/BIA-BQM/31981/2017 PD/BD/114445/2016 UID/Multi/04378/2019 ROTEIRO/0031/2013 -PINFRA/22161/2016The monoheme outer membrane cytochrome F (OmcF) from Geobacter sulfurreducens plays an important role in Fe(III) reduction and electric current production. The electrochemical characterization of this cytochrome has shown that its redox potential is modulated by the solution pH (redox-Bohr effect) endowing the protein with the necessary properties to couple electron and proton transfer in the physiological range. The analysis of the OmcF structures in the reduced and oxidized states showed that with the exception of the side chain of histidine 47 (His47), all other residues with protonatable side chains are distant from the heme iron and, therefore, are unlikely to affect the redox potential of the protein. The protonatable site at the imidazole ring of His47 is in the close proximity to the heme and, therefore, this residue was suggested as the redox-Bohr center. In the present work, we tested this hypothesis by replacing the His47 with non-protonatable residues (isoleucine – OmcFH47I and phenylalanine – OmcFH47F). The structure of the mutant OmcFH47I was determined by X-ray crystallography to 1.13 Å resolution and showed only minimal changes at the site of the mutation. Both mutants were 15N-labeled and their overall folding was confirmed to be the same as the wild-type by NMR spectroscopy. The pH dependence of the redox potential of the mutants was measured by cyclic voltammetry. Compared to the wild-type protein, the magnitude of the redox-Bohr effect in the mutants was smaller, but not fully abolished, confirming the role of His47 on the pH modulation of OmcF’s redox potential. However, the pH effect on the heme substituents’ NMR chemical shifts suggested that the heme propionate P13 also contributes to the overall redox-Bohr effect in OmcF. In physiological terms, the contribution of two independent acid–base centers to the observed redox-Bohr effect confers OmcF a higher versatility to environmental changes by coupling electron/proton transfer within a wider pH range.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaLAQV@REQUIMTERUNTeixeira, Liliana R.Cordas, Cristina M.Fonseca, Marta P.Duke, Norma E. C.Pokkuluri, Phani RajSalgueiro, Carlos A.2021-05-04T22:52:22Z2020-01-142020-01-14T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/117015eng1664-302XPURE: 16762828https://doi.org/10.3389/fmicb.2019.02941info: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:RCAAP2024-03-11T04:59:55Zoai:run.unl.pt:10362/117015Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:43:25.277743Repositório 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 Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
title Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
spellingShingle Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
Teixeira, Liliana R.
c-type cytochrome
cyclic voltammetry
electron transfer proteins
nuclear magnetic resonance
redox-Bohr effect
site-directed mutagenesis
X-ray crystallography
Microbiology
Microbiology (medical)
title_short Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
title_full Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
title_fullStr Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
title_full_unstemmed Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
title_sort Modulation of the Redox Potential and Electron/Proton Transfer Mechanisms in the Outer Membrane Cytochrome OmcF From Geobacter sulfurreducens
author Teixeira, Liliana R.
author_facet Teixeira, Liliana R.
Cordas, Cristina M.
Fonseca, Marta P.
Duke, Norma E. C.
Pokkuluri, Phani Raj
Salgueiro, Carlos A.
author_role author
author2 Cordas, Cristina M.
Fonseca, Marta P.
Duke, Norma E. C.
Pokkuluri, Phani Raj
Salgueiro, Carlos A.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv UCIBIO - Applied Molecular Biosciences Unit
DQ - Departamento de Química
LAQV@REQUIMTE
RUN
dc.contributor.author.fl_str_mv Teixeira, Liliana R.
Cordas, Cristina M.
Fonseca, Marta P.
Duke, Norma E. C.
Pokkuluri, Phani Raj
Salgueiro, Carlos A.
dc.subject.por.fl_str_mv c-type cytochrome
cyclic voltammetry
electron transfer proteins
nuclear magnetic resonance
redox-Bohr effect
site-directed mutagenesis
X-ray crystallography
Microbiology
Microbiology (medical)
topic c-type cytochrome
cyclic voltammetry
electron transfer proteins
nuclear magnetic resonance
redox-Bohr effect
site-directed mutagenesis
X-ray crystallography
Microbiology
Microbiology (medical)
description PD/00193/2012 UID/FIS/00068/2019 PTDC/BBBBQB/3554/2014 PTDC/BIA-BQM/31981/2017 PD/BD/114445/2016 UID/Multi/04378/2019 ROTEIRO/0031/2013 -PINFRA/22161/2016
publishDate 2020
dc.date.none.fl_str_mv 2020-01-14
2020-01-14T00:00:00Z
2021-05-04T22:52:22Z
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/10362/117015
url http://hdl.handle.net/10362/117015
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1664-302X
PURE: 16762828
https://doi.org/10.3389/fmicb.2019.02941
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
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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