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

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 b...

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Autor principal: Todorovie, S.
Otros Autores: Verissimo, A., Wisitruangsakul, N., Zebger, I., Hildebrandt, P., Pereira, M.M, Teixeira, M., Murgida, D.H
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: American Chemical Society 2008
Acceso en línea:Registro en Scopus
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030 |a JPCBF 
100 1 |a Todorovie, S. 
245 1 0 |a SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct 
260 |b American Chemical Society  |c 2008 
270 1 0 |m Todorovie, S.; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, EAN, 2780-157 Oeiras, Portugal; email: smilja@itqb.unl.pt 
506 |2 openaire  |e Política editorial 
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520 3 |a 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.  |l eng 
593 |a Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, EAN, 2780-157 Oeiras, Portugal 
593 |a Max-Volmer-Laboratorium für Biophysikalische Chemie, Institut Für Chemie, Technische Universitat Berlin, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany 
593 |a 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 
690 1 0 |a BIOMIMETICS 
690 1 0 |a COORDINATION REACTIONS 
690 1 0 |a CYCLIC VOLTAMMETRY 
690 1 0 |a ENZYMES 
690 1 0 |a HEMOGLOBIN 
690 1 0 |a LIPID BILAYERS 
690 1 0 |a OXYGEN 
690 1 0 |a PORPHYRINS 
690 1 0 |a SILVER 
690 1 0 |a SPECTROELECTROCHEMISTRY 
690 1 0 |a VOLUMETRIC ANALYSIS 
690 1 0 |a BRADYRHIZOBIUM JAPONICUM 
690 1 0 |a CATALYTIC ACTIVITIES 
690 1 0 |a ENERGY TRANSDUCTIONS 
690 1 0 |a IMMOBILIZED ENZYMES 
690 1 0 |a IN-SITU 
690 1 0 |a NANOSTRUCTURED 
690 1 0 |a NATIVE STRUCTURES 
690 1 0 |a REDUCTION POTENTIALS 
690 1 0 |a SILVER ELECTRODES 
690 1 0 |a SPECTROELECTROCHEMICAL STUDIES 
690 1 0 |a SPECTROELECTROCHEMICAL TITRATIONS 
690 1 0 |a ENZYME ACTIVITY 
700 1 |a Verissimo, A. 
700 1 |a Wisitruangsakul, N. 
700 1 |a Zebger, I. 
700 1 |a Hildebrandt, P. 
700 1 |a Pereira, M.M. 
700 1 |a Teixeira, M. 
700 1 |a Murgida, D.H. 
773 0 |d American Chemical Society, 2008  |g v. 112  |h pp. 16952-16959  |k n. 51  |p J Phys Chem B  |x 15206106  |w (AR-BaUEN)CENRE-5879  |t Journal of Physical Chemistry B 
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