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Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors
Heme peroxidases are widely used as biological recognition elements in electrochemical biosensors for hydrogen peroxide and phenolic compounds. Various nature-derived and fully synthetic heme peroxidase mimics have been designed and their potential for replacing the natural enzymes in biosensors has...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7374321/ https://www.ncbi.nlm.nih.gov/pubmed/32630267 http://dx.doi.org/10.3390/s20133692 |
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author | Neumann, Bettina Wollenberger, Ulla |
author_facet | Neumann, Bettina Wollenberger, Ulla |
author_sort | Neumann, Bettina |
collection | PubMed |
description | Heme peroxidases are widely used as biological recognition elements in electrochemical biosensors for hydrogen peroxide and phenolic compounds. Various nature-derived and fully synthetic heme peroxidase mimics have been designed and their potential for replacing the natural enzymes in biosensors has been investigated. The use of semiconducting materials as transducers can thereby offer new opportunities with respect to catalyst immobilization, reaction stimulation, or read-out. This review focuses on approaches for the construction of electrochemical biosensors employing natural heme peroxidases as well as various mimics immobilized on semiconducting electrode surfaces. It will outline important advances made so far as well as the novel applications resulting thereof. |
format | Online Article Text |
id | pubmed-7374321 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-73743212020-08-06 Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors Neumann, Bettina Wollenberger, Ulla Sensors (Basel) Review Heme peroxidases are widely used as biological recognition elements in electrochemical biosensors for hydrogen peroxide and phenolic compounds. Various nature-derived and fully synthetic heme peroxidase mimics have been designed and their potential for replacing the natural enzymes in biosensors has been investigated. The use of semiconducting materials as transducers can thereby offer new opportunities with respect to catalyst immobilization, reaction stimulation, or read-out. This review focuses on approaches for the construction of electrochemical biosensors employing natural heme peroxidases as well as various mimics immobilized on semiconducting electrode surfaces. It will outline important advances made so far as well as the novel applications resulting thereof. MDPI 2020-07-01 /pmc/articles/PMC7374321/ /pubmed/32630267 http://dx.doi.org/10.3390/s20133692 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Neumann, Bettina Wollenberger, Ulla Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors |
title | Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors |
title_full | Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors |
title_fullStr | Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors |
title_full_unstemmed | Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors |
title_short | Electrochemical Biosensors Employing Natural and Artificial Heme Peroxidases on Semiconductors |
title_sort | electrochemical biosensors employing natural and artificial heme peroxidases on semiconductors |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7374321/ https://www.ncbi.nlm.nih.gov/pubmed/32630267 http://dx.doi.org/10.3390/s20133692 |
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