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Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces

The immobilization of redox proteins or enzymes onto conductive surfaces has application in the analysis of biological processes, the fabrication of biosensors, and in the development of green technologies and biochemical synthetic approaches. This review evaluates the methods through which redox pr...

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Detalles Bibliográficos
Autores principales: Yates, Nicholas D. J., Fascione, Martin A., Parkin, Alison
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6120495/
https://www.ncbi.nlm.nih.gov/pubmed/29637638
http://dx.doi.org/10.1002/chem.201800750
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author Yates, Nicholas D. J.
Fascione, Martin A.
Parkin, Alison
author_facet Yates, Nicholas D. J.
Fascione, Martin A.
Parkin, Alison
author_sort Yates, Nicholas D. J.
collection PubMed
description The immobilization of redox proteins or enzymes onto conductive surfaces has application in the analysis of biological processes, the fabrication of biosensors, and in the development of green technologies and biochemical synthetic approaches. This review evaluates the methods through which redox proteins can be attached to electrode surfaces in a “wired” configuration, that is, one that facilitates direct electron transfer. The feasibility of simple electroactive adsorption onto a range of electrode surfaces is illustrated, with a highlight on the recent advances that have been achieved in biotechnological device construction using carbon materials and metal oxides. The covalent crosslinking strategies commonly used for the modification and biofunctionalization of electrode surfaces are also evaluated. Recent innovations in harnessing chemical biology methods for electrically wiring redox biology to surfaces are emphasized.
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spelling pubmed-61204952018-09-05 Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces Yates, Nicholas D. J. Fascione, Martin A. Parkin, Alison Chemistry Reviews The immobilization of redox proteins or enzymes onto conductive surfaces has application in the analysis of biological processes, the fabrication of biosensors, and in the development of green technologies and biochemical synthetic approaches. This review evaluates the methods through which redox proteins can be attached to electrode surfaces in a “wired” configuration, that is, one that facilitates direct electron transfer. The feasibility of simple electroactive adsorption onto a range of electrode surfaces is illustrated, with a highlight on the recent advances that have been achieved in biotechnological device construction using carbon materials and metal oxides. The covalent crosslinking strategies commonly used for the modification and biofunctionalization of electrode surfaces are also evaluated. Recent innovations in harnessing chemical biology methods for electrically wiring redox biology to surfaces are emphasized. John Wiley and Sons Inc. 2018-06-06 2018-08-22 /pmc/articles/PMC6120495/ /pubmed/29637638 http://dx.doi.org/10.1002/chem.201800750 Text en © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Reviews
Yates, Nicholas D. J.
Fascione, Martin A.
Parkin, Alison
Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
title Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
title_full Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
title_fullStr Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
title_full_unstemmed Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
title_short Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode Surfaces
title_sort methodologies for “wiring” redox proteins/enzymes to electrode surfaces
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6120495/
https://www.ncbi.nlm.nih.gov/pubmed/29637638
http://dx.doi.org/10.1002/chem.201800750
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