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dc.contributor.author
Todorovie, Smilja
dc.contributor.author
Verissimo, Andreia
dc.contributor.author
Wisitruangsakul, Nattwandee
dc.contributor.author
Zebger, Ingo
dc.contributor.author
Hildebrandt, Peter
dc.contributor.author
Pereira, Manuela M.
dc.contributor.author
Teixeira, Miguel
dc.contributor.author
Murgida, Daniel Horacio
dc.date.available
2019-09-17T22:23:51Z
dc.date.issued
2008-12
dc.identifier.citation
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
dc.identifier.issn
1089-5647
dc.identifier.uri
http://hdl.handle.net/11336/83796
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Oxygen Reductases
dc.subject
Respiration
dc.subject
Raman
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Electron Transfer
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica
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Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-06-11T18:14:32Z
dc.identifier.eissn
1520-6106
dc.journal.volume
112
dc.journal.number
51
dc.journal.pagination
16952-16959
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Todorovie, Smilja. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Verissimo, Andreia. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Wisitruangsakul, Nattwandee. Technishe Universitat Berlin; Alemania
dc.description.fil
Fil: Zebger, Ingo. Technishe Universitat Berlin; Alemania
dc.description.fil
Fil: Hildebrandt, Peter. Technishe Universitat Berlin; Alemania
dc.description.fil
Fil: Pereira, Manuela M.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Teixeira, Miguel. Universidade Nova de Lisboa; Portugal
dc.description.fil
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
dc.journal.title
Journal of Physical Chemistry B
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/full/10.1021/jp807862m
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1021/jp807862m
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