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Todorovie, S.; Verissimo, A.; Wisitruangsakul, N.; Zebger, I.; Hildebrandt, P.; Pereira, M.M.; Teixeira, M.; Murgida, D.H. "SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct" (2008) Journal of Physical Chemistry B. 112(51):16952-16959
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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. © 2008 American Chemical Society.

Registro:

Documento: Artículo
Título:SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
Autor:Todorovie, S.; Verissimo, A.; Wisitruangsakul, N.; Zebger, I.; Hildebrandt, P.; Pereira, M.M.; Teixeira, M.; Murgida, D.H.
Filiación:Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, EAN, 2780-157 Oeiras, Portugal
Max-Volmer-Laboratorium für Biophysikalische Chemie, Institut Für Chemie, Technische Universitat Berlin, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany
Departamento de Quimica Inorganica, Analitica y Quimica Fisica/INQUIMAE, Facultad de Ciencias Exactas y Naturales, Ciudad Universiraria, Pab. 2, piso 1, C1428EHA Buenos Aires, Argentina
Palabras clave:Biomimetics; Coordination reactions; Cyclic voltammetry; Enzymes; Hemoglobin; Lipid bilayers; Oxygen; Porphyrins; Silver; Spectroelectrochemistry; Volumetric analysis; Bradyrhizobium japonicum; Catalytic activities; Energy transductions; Immobilized enzymes; In-situ; Nanostructured; Native structures; Reduction potentials; Silver electrodes; Spectroelectrochemical studies; Spectroelectrochemical titrations; Enzyme activity
Año:2008
Volumen:112
Número:51
Página de inicio:16952
Página de fin:16959
DOI: http://dx.doi.org/10.1021/jp807862m
Título revista:Journal of Physical Chemistry B
Título revista abreviado:J Phys Chem B
ISSN:15206106
CODEN:JPCBF
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v112_n51_p16952_Todorovie

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Citas:

---------- APA ----------
Todorovie, S., Verissimo, A., Wisitruangsakul, N., Zebger, I., Hildebrandt, P., Pereira, M.M., Teixeira, M.,..., Murgida, D.H. (2008) . SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct. Journal of Physical Chemistry B, 112(51), 16952-16959.
http://dx.doi.org/10.1021/jp807862m
---------- CHICAGO ----------
Todorovie, S., Verissimo, A., Wisitruangsakul, N., Zebger, I., Hildebrandt, P., Pereira, M.M., et al. "SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct" . Journal of Physical Chemistry B 112, no. 51 (2008) : 16952-16959.
http://dx.doi.org/10.1021/jp807862m
---------- MLA ----------
Todorovie, S., Verissimo, A., Wisitruangsakul, N., Zebger, I., Hildebrandt, P., Pereira, M.M., et al. "SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct" . Journal of Physical Chemistry B, vol. 112, no. 51, 2008, pp. 16952-16959.
http://dx.doi.org/10.1021/jp807862m
---------- VANCOUVER ----------
Todorovie, S., Verissimo, A., Wisitruangsakul, N., Zebger, I., Hildebrandt, P., Pereira, M.M., et al. SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct. J Phys Chem B. 2008;112(51):16952-16959.
http://dx.doi.org/10.1021/jp807862m