Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes

For the first time, respiratory complex I has been reconstituted on an electrode preserving its structure and activity. Respiratory complex I is a membrane-bound enzyme that has an essential function in cellular energy production. It couples NADH:quinone oxidoreduction to translocation of ions acros...

ver descrição completa

Detalhes bibliográficos
Autores: Gutiérrez-Sanz, Óscar, Olea, David, Pita, Marcos, Batista, Ana P., Alonso Caballero, Álvaro, Pereira, Manuela M., Vélez, Marisela, López de Lacey, Antonio
Formato: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2014
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/142779
Acesso em linha:http://hdl.handle.net/10261/142779
Access Level:acceso abierto
Palavra-chave:Infrared-absorption spectroscopy
Nadh-Ubiquinone oxidoreductase
Escherichia-coli
Rhodothermus-marinus
Lipid-membrane
Cluster N2
Electrochemistry
Oxidation
Transport
Bilayer
Adenosinetriphosphate
Atomic force microscopy
Biomimetics
Cell membranes
Electrodes
Gold
Organic polymers
Self assembled monolayers
Electrochemical measurements
Electrochemical potential
Membrane-bound enzymes
Mitochondrial membranes
Proton translocation
Respiratory complex
Structure and activities
Thiol self-assembled monolayers
Gold compounds
Artificial membranes
Bacterial proteins
Biomimetic materials
Proton
Reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone)
Thiol reagent
Chemistry
Electrode
Electron transport
Enzymology
Isolation and purification
Rhodothermus
Electron Transport Complex I
Membranes, Artificial
Microscopy, Atomic Force
Protons
Sulfhydryl Reagents
id ES_38dc679f0763e1541e9dfd95438ab408
oai_identifier_str oai:digital.csic.es:10261/142779
network_acronym_str ES
network_name_str España
repository_id_str
spelling Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodesGutiérrez-Sanz, ÓscarOlea, DavidPita, MarcosBatista, Ana P.Alonso Caballero, ÁlvaroPereira, Manuela M.Vélez, MariselaLópez de Lacey, AntonioInfrared-absorption spectroscopyNadh-Ubiquinone oxidoreductaseEscherichia-coliRhodothermus-marinusLipid-membraneCluster N2ElectrochemistryOxidationTransportBilayerAdenosinetriphosphateAtomic force microscopyBiomimeticsCell membranesElectrodesGoldOrganic polymersSelf assembled monolayersElectrochemical measurementsElectrochemical potentialMembrane-bound enzymesMitochondrial membranesProton translocationRespiratory complexStructure and activitiesThiol self-assembled monolayersGold compoundsArtificial membranesBacterial proteinsBiomimetic materialsProtonAtomic force microscopyReduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone)Thiol reagentChemistryElectrodeElectron transportEnzymologyIsolation and purificationRhodothermusBacterial proteinsBiomimetic materialsElectrodesElectron transportElectron Transport Complex IMembranes, ArtificialMicroscopy, Atomic ForceProtonsRhodothermusSulfhydryl ReagentsFor the first time, respiratory complex I has been reconstituted on an electrode preserving its structure and activity. Respiratory complex I is a membrane-bound enzyme that has an essential function in cellular energy production. It couples NADH:quinone oxidoreduction to translocation of ions across the cellular (in prokaryotes) or mitochondrial membranes. Therefore, complex I contributes to the establishment and maintenance of the transmembrane difference of electrochemical potential required for adenosine triphosphate synthesis, transport, and motility. Our new strategy has been applied for reconstituting the bacterial complex I from Rhodothermus marinus onto a biomimetic membrane supported on gold electrodes modified with a thiol self-assembled monolayer (SAM). Atomic force microscopy and faradaic impedance measurements give evidence of the biomimetic construction, whereas electrochemical measurements show its functionality. Both electron transfer and proton translocation by respiratory complex I were monitored, simulating in vivo conditions. © 2014 American Chemical Society.This work was funded by the Spanish MINECO (project CTQ2012-32448) and by Fundação para a Ciência e a Tecnologia (PTDC/BBB-BQB/2294/2012 to M.M.P.). The work was also supported by Fundação para a Ciência e a Tecnologia through grant # PEst-OE/EQB/LA0004/2011. M.P. and O.G.-S. acknowledge the Ramon y Cajal and the FPI programs respectively from the Spanish MINECO. A.P.B. is recipient of a grant from Fundação para a Ciência e a Tecnologia (SFRH/BPD/80741/2011).Peer ReviewedAmerican Chemical SocietyMinisterio de Economía y Competitividad (España)Fundação para a Ciência e a Tecnologia (Portugal)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2017201720142017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/142779reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://doi.org/10.1021/la501825rSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1427792026-05-22T06:33:51Z
dc.title.none.fl_str_mv Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
title Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
spellingShingle Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
Gutiérrez-Sanz, Óscar
Infrared-absorption spectroscopy
Nadh-Ubiquinone oxidoreductase
Escherichia-coli
Rhodothermus-marinus
Lipid-membrane
Cluster N2
Electrochemistry
Oxidation
Transport
Bilayer
Adenosinetriphosphate
Atomic force microscopy
Biomimetics
Cell membranes
Electrodes
Gold
Organic polymers
Self assembled monolayers
Electrochemical measurements
Electrochemical potential
Membrane-bound enzymes
Mitochondrial membranes
Proton translocation
Respiratory complex
Structure and activities
Thiol self-assembled monolayers
Gold compounds
Artificial membranes
Bacterial proteins
Biomimetic materials
Proton
Atomic force microscopy
Reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone)
Thiol reagent
Chemistry
Electrode
Electron transport
Enzymology
Isolation and purification
Rhodothermus
Bacterial proteins
Biomimetic materials
Electrodes
Electron transport
Electron Transport Complex I
Membranes, Artificial
Microscopy, Atomic Force
Protons
Rhodothermus
Sulfhydryl Reagents
title_short Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
title_full Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
title_fullStr Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
title_full_unstemmed Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
title_sort Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
dc.creator.none.fl_str_mv Gutiérrez-Sanz, Óscar
Olea, David
Pita, Marcos
Batista, Ana P.
Alonso Caballero, Álvaro
Pereira, Manuela M.
Vélez, Marisela
López de Lacey, Antonio
author Gutiérrez-Sanz, Óscar
author_facet Gutiérrez-Sanz, Óscar
Olea, David
Pita, Marcos
Batista, Ana P.
Alonso Caballero, Álvaro
Pereira, Manuela M.
Vélez, Marisela
López de Lacey, Antonio
author_role author
author2 Olea, David
Pita, Marcos
Batista, Ana P.
Alonso Caballero, Álvaro
Pereira, Manuela M.
Vélez, Marisela
López de Lacey, Antonio
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Fundação para a Ciência e a Tecnologia (Portugal)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Infrared-absorption spectroscopy
Nadh-Ubiquinone oxidoreductase
Escherichia-coli
Rhodothermus-marinus
Lipid-membrane
Cluster N2
Electrochemistry
Oxidation
Transport
Bilayer
Adenosinetriphosphate
Atomic force microscopy
Biomimetics
Cell membranes
Electrodes
Gold
Organic polymers
Self assembled monolayers
Electrochemical measurements
Electrochemical potential
Membrane-bound enzymes
Mitochondrial membranes
Proton translocation
Respiratory complex
Structure and activities
Thiol self-assembled monolayers
Gold compounds
Artificial membranes
Bacterial proteins
Biomimetic materials
Proton
Atomic force microscopy
Reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone)
Thiol reagent
Chemistry
Electrode
Electron transport
Enzymology
Isolation and purification
Rhodothermus
Bacterial proteins
Biomimetic materials
Electrodes
Electron transport
Electron Transport Complex I
Membranes, Artificial
Microscopy, Atomic Force
Protons
Rhodothermus
Sulfhydryl Reagents
topic Infrared-absorption spectroscopy
Nadh-Ubiquinone oxidoreductase
Escherichia-coli
Rhodothermus-marinus
Lipid-membrane
Cluster N2
Electrochemistry
Oxidation
Transport
Bilayer
Adenosinetriphosphate
Atomic force microscopy
Biomimetics
Cell membranes
Electrodes
Gold
Organic polymers
Self assembled monolayers
Electrochemical measurements
Electrochemical potential
Membrane-bound enzymes
Mitochondrial membranes
Proton translocation
Respiratory complex
Structure and activities
Thiol self-assembled monolayers
Gold compounds
Artificial membranes
Bacterial proteins
Biomimetic materials
Proton
Atomic force microscopy
Reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone)
Thiol reagent
Chemistry
Electrode
Electron transport
Enzymology
Isolation and purification
Rhodothermus
Bacterial proteins
Biomimetic materials
Electrodes
Electron transport
Electron Transport Complex I
Membranes, Artificial
Microscopy, Atomic Force
Protons
Rhodothermus
Sulfhydryl Reagents
description For the first time, respiratory complex I has been reconstituted on an electrode preserving its structure and activity. Respiratory complex I is a membrane-bound enzyme that has an essential function in cellular energy production. It couples NADH:quinone oxidoreduction to translocation of ions across the cellular (in prokaryotes) or mitochondrial membranes. Therefore, complex I contributes to the establishment and maintenance of the transmembrane difference of electrochemical potential required for adenosine triphosphate synthesis, transport, and motility. Our new strategy has been applied for reconstituting the bacterial complex I from Rhodothermus marinus onto a biomimetic membrane supported on gold electrodes modified with a thiol self-assembled monolayer (SAM). Atomic force microscopy and faradaic impedance measurements give evidence of the biomimetic construction, whereas electrochemical measurements show its functionality. Both electron transfer and proton translocation by respiratory complex I were monitored, simulating in vivo conditions. © 2014 American Chemical Society.
publishDate 2014
dc.date.none.fl_str_mv 2014
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/142779
url http://hdl.handle.net/10261/142779
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://doi.org/10.1021/la501825r

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869406128724508672
score 15,81155