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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Detalles Bibliográficos
Autor principal: Murgida, Daniel Horacio
Publicado: 2008
Materias:
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
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v112_n51_p16952_Todorovie
http://hdl.handle.net/20.500.12110/paper_15206106_v112_n51_p16952_Todorovie
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_15206106_v112_n51_p16952_Todorovie
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spelling paper:paper_15206106_v112_n51_p16952_Todorovie2023-06-08T16:19:00Z SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct Murgida, Daniel Horacio 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 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. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v112_n51_p16952_Todorovie http://hdl.handle.net/20.500.12110/paper_15206106_v112_n51_p16952_Todorovie
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic 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
spellingShingle 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
Murgida, Daniel Horacio
SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
topic_facet 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
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. © 2008 American Chemical Society.
author Murgida, Daniel Horacio
author_facet Murgida, Daniel Horacio
author_sort Murgida, Daniel Horacio
title SERR-spectroelectrochemical study of a cbb oxygen redutase in a biomimetic construct
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
publishDate 2008
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v112_n51_p16952_Todorovie
http://hdl.handle.net/20.500.12110/paper_15206106_v112_n51_p16952_Todorovie
work_keys_str_mv AT murgidadanielhoracio serrspectroelectrochemicalstudyofacbboxygenredutaseinabiomimeticconstruct
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