SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct

Autores
Todorovie, Smilja; Verissimo, Andreia; Wisitruangsakul, Nattwandee; Zebger, Ingo; Hildebrandt, Peter; Pereira, Manuela M.; Teixeira, Miguel; Murgida, Daniel Horacio
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The chb3 oxygen reductase from Bradyrhizobium japonicum was immobilized on nanostructured silver electrodes by anchoring the enzyme via a His-tag to a Ni-NTA coating, followed by reconstitution of a lipid bilayer. The immobilized enzyme retains the native structure and catalytic activity as judged by in situ surface- enhanced vibrational spectroscopy and cyclic voltammetry, respectively. Spectroelectrochemical titrations followed by SERR spectroscopy of the integral enzyme and its monohemic (fixO) and dihemic subunits (fixP), allowed the determination of the reduction potentials for the different heme c groups. Both in the isolated subunits and in the integral enzyme the Met/His-coordinated hemes from the two subunits present identical reduction potentials of 180 mV, whereas for the bis-His heme from fixP the value is ca. 400 mV. The determination of reduction potentials of the individual hemes c reported in this work provides the basis for further exploring the mechanism of electroprotonic energy transduction of this complex enzyme.
Fil: Todorovie, Smilja. Universidade Nova de Lisboa; Portugal
Fil: Verissimo, Andreia. Universidade Nova de Lisboa; Portugal
Fil: Wisitruangsakul, Nattwandee. Technishe Universitat Berlin; Alemania
Fil: Zebger, Ingo. Technishe Universitat Berlin; Alemania
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
Fil: Pereira, Manuela M.. Universidade Nova de Lisboa; Portugal
Fil: Teixeira, Miguel. Universidade Nova de Lisboa; Portugal
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina
Materia
Oxygen Reductases
Respiration
Raman
Electron Transfer
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/83796
Acceder
id CONICETDig_ce41dc8fceb50dcfedbd2c2bd7636417
oai_identifier_str oai:ri.conicet.gov.ar:11336/83796
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic constructTodorovie, SmiljaVerissimo, AndreiaWisitruangsakul, NattwandeeZebger, IngoHildebrandt, PeterPereira, Manuela M.Teixeira, MiguelMurgida, Daniel HoracioOxygen ReductasesRespirationRamanElectron Transferhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The chb3 oxygen reductase from Bradyrhizobium japonicum was immobilized on nanostructured silver electrodes by anchoring the enzyme via a His-tag to a Ni-NTA coating, followed by reconstitution of a lipid bilayer. The immobilized enzyme retains the native structure and catalytic activity as judged by in situ surface- enhanced vibrational spectroscopy and cyclic voltammetry, respectively. Spectroelectrochemical titrations followed by SERR spectroscopy of the integral enzyme and its monohemic (fixO) and dihemic subunits (fixP), allowed the determination of the reduction potentials for the different heme c groups. Both in the isolated subunits and in the integral enzyme the Met/His-coordinated hemes from the two subunits present identical reduction potentials of 180 mV, whereas for the bis-His heme from fixP the value is ca. 400 mV. The determination of reduction potentials of the individual hemes c reported in this work provides the basis for further exploring the mechanism of electroprotonic energy transduction of this complex enzyme.Fil: Todorovie, Smilja. Universidade Nova de Lisboa; PortugalFil: Verissimo, Andreia. Universidade Nova de Lisboa; PortugalFil: Wisitruangsakul, Nattwandee. Technishe Universitat Berlin; AlemaniaFil: Zebger, Ingo. Technishe Universitat Berlin; AlemaniaFil: Hildebrandt, Peter. Technishe Universitat Berlin; AlemaniaFil: Pereira, Manuela M.. Universidade Nova de Lisboa; PortugalFil: Teixeira, Miguel. Universidade Nova de Lisboa; PortugalFil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; ArgentinaAmerican Chemical Society2008-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/83796Todorovie, Smilja; Verissimo, Andreia; Wisitruangsakul, Nattwandee; Zebger, Ingo; Hildebrandt, Peter; et al.; SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct; American Chemical Society; Journal of Physical Chemistry B; 112; 51; 12-2008; 16952-169591089-56471520-6106CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/full/10.1021/jp807862minfo:eu-repo/semantics/altIdentifier/doi/10.1021/jp807862minfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:54:54Zoai:ri.conicet.gov.ar:11336/83796instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:54:54.967CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
title SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
spellingShingle SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
Todorovie, Smilja
Oxygen Reductases
Respiration
Raman
Electron Transfer
title_short SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
title_full SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
title_fullStr SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
title_full_unstemmed SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
title_sort SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
dc.creator.none.fl_str_mv Todorovie, Smilja
Verissimo, Andreia
Wisitruangsakul, Nattwandee
Zebger, Ingo
Hildebrandt, Peter
Pereira, Manuela M.
Teixeira, Miguel
Murgida, Daniel Horacio
author Todorovie, Smilja
author_facet Todorovie, Smilja
Verissimo, Andreia
Wisitruangsakul, Nattwandee
Zebger, Ingo
Hildebrandt, Peter
Pereira, Manuela M.
Teixeira, Miguel
Murgida, Daniel Horacio
author_role author
author2 Verissimo, Andreia
Wisitruangsakul, Nattwandee
Zebger, Ingo
Hildebrandt, Peter
Pereira, Manuela M.
Teixeira, Miguel
Murgida, Daniel Horacio
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Oxygen Reductases
Respiration
Raman
Electron Transfer
topic Oxygen Reductases
Respiration
Raman
Electron Transfer
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The chb3 oxygen reductase from Bradyrhizobium japonicum was immobilized on nanostructured silver electrodes by anchoring the enzyme via a His-tag to a Ni-NTA coating, followed by reconstitution of a lipid bilayer. The immobilized enzyme retains the native structure and catalytic activity as judged by in situ surface- enhanced vibrational spectroscopy and cyclic voltammetry, respectively. Spectroelectrochemical titrations followed by SERR spectroscopy of the integral enzyme and its monohemic (fixO) and dihemic subunits (fixP), allowed the determination of the reduction potentials for the different heme c groups. Both in the isolated subunits and in the integral enzyme the Met/His-coordinated hemes from the two subunits present identical reduction potentials of 180 mV, whereas for the bis-His heme from fixP the value is ca. 400 mV. The determination of reduction potentials of the individual hemes c reported in this work provides the basis for further exploring the mechanism of electroprotonic energy transduction of this complex enzyme.
Fil: Todorovie, Smilja. Universidade Nova de Lisboa; Portugal
Fil: Verissimo, Andreia. Universidade Nova de Lisboa; Portugal
Fil: Wisitruangsakul, Nattwandee. Technishe Universitat Berlin; Alemania
Fil: Zebger, Ingo. Technishe Universitat Berlin; Alemania
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
Fil: Pereira, Manuela M.. Universidade Nova de Lisboa; Portugal
Fil: Teixeira, Miguel. Universidade Nova de Lisboa; Portugal
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Inorgánica, Analítica y Química Física; Argentina
description The chb3 oxygen reductase from Bradyrhizobium japonicum was immobilized on nanostructured silver electrodes by anchoring the enzyme via a His-tag to a Ni-NTA coating, followed by reconstitution of a lipid bilayer. The immobilized enzyme retains the native structure and catalytic activity as judged by in situ surface- enhanced vibrational spectroscopy and cyclic voltammetry, respectively. Spectroelectrochemical titrations followed by SERR spectroscopy of the integral enzyme and its monohemic (fixO) and dihemic subunits (fixP), allowed the determination of the reduction potentials for the different heme c groups. Both in the isolated subunits and in the integral enzyme the Met/His-coordinated hemes from the two subunits present identical reduction potentials of 180 mV, whereas for the bis-His heme from fixP the value is ca. 400 mV. The determination of reduction potentials of the individual hemes c reported in this work provides the basis for further exploring the mechanism of electroprotonic energy transduction of this complex enzyme.
publishDate 2008
dc.date.none.fl_str_mv 2008-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/83796
Todorovie, Smilja; Verissimo, Andreia; Wisitruangsakul, Nattwandee; Zebger, Ingo; Hildebrandt, Peter; et al.; SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct; American Chemical Society; Journal of Physical Chemistry B; 112; 51; 12-2008; 16952-16959
1089-5647
1520-6106
CONICET Digital
CONICET
url http://hdl.handle.net/11336/83796
identifier_str_mv Todorovie, Smilja; Verissimo, Andreia; Wisitruangsakul, Nattwandee; Zebger, Ingo; Hildebrandt, Peter; et al.; SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct; American Chemical Society; Journal of Physical Chemistry B; 112; 51; 12-2008; 16952-16959
1089-5647
1520-6106
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/full/10.1021/jp807862m
info:eu-repo/semantics/altIdentifier/doi/10.1021/jp807862m
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846782249467379712
score 12.982451

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