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In Situ Spectroelectrochemical Investigations of Electrode-Confined Electron-Transferring Proteins and Redox Enzymes
[Image: see text] This perspective analyzes recent advances in the spectroelectrochemical investigation of redox proteins and enzymes immobilized on biocompatible or biomimetic electrode surfaces. Specifically, the article highlights new insights obtained by surface-enhanced resonance Raman (SERR),...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7876673/ https://www.ncbi.nlm.nih.gov/pubmed/33585730 http://dx.doi.org/10.1021/acsomega.0c05746 |
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author | Murgida, Daniel H. |
author_facet | Murgida, Daniel H. |
author_sort | Murgida, Daniel H. |
collection | PubMed |
description | [Image: see text] This perspective analyzes recent advances in the spectroelectrochemical investigation of redox proteins and enzymes immobilized on biocompatible or biomimetic electrode surfaces. Specifically, the article highlights new insights obtained by surface-enhanced resonance Raman (SERR), surface-enhanced infrared absorption (SEIRA), protein film infrared electrochemistry (PFIRE), polarization modulation infrared reflection–absorption spectroscopy (PMIRRAS), Förster resonance energy transfer (FRET), X-ray absorption spectroscopy (XAS), electron paramagnetic resonance (EPR), and differential electrochemical mass spectrometry (DMES)-based spectroelectrochemical methods on the structure, orientation, dynamics, and reaction mechanisms for a variety of immobilized species. This includes small heme and copper electron shuttling proteins, large respiratory complexes, hydrogenases, multicopper oxidases, alcohol dehydrogenases, endonucleases, NO-reductases, and dye decolorizing peroxidases, among other enzymes. Finally, I discuss the challenges and foreseeable future developments toward a better understanding of the functioning of these complex macromolecules and their exploitation in technological devices. |
format | Online Article Text |
id | pubmed-7876673 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-78766732021-02-12 In Situ Spectroelectrochemical Investigations of Electrode-Confined Electron-Transferring Proteins and Redox Enzymes Murgida, Daniel H. ACS Omega [Image: see text] This perspective analyzes recent advances in the spectroelectrochemical investigation of redox proteins and enzymes immobilized on biocompatible or biomimetic electrode surfaces. Specifically, the article highlights new insights obtained by surface-enhanced resonance Raman (SERR), surface-enhanced infrared absorption (SEIRA), protein film infrared electrochemistry (PFIRE), polarization modulation infrared reflection–absorption spectroscopy (PMIRRAS), Förster resonance energy transfer (FRET), X-ray absorption spectroscopy (XAS), electron paramagnetic resonance (EPR), and differential electrochemical mass spectrometry (DMES)-based spectroelectrochemical methods on the structure, orientation, dynamics, and reaction mechanisms for a variety of immobilized species. This includes small heme and copper electron shuttling proteins, large respiratory complexes, hydrogenases, multicopper oxidases, alcohol dehydrogenases, endonucleases, NO-reductases, and dye decolorizing peroxidases, among other enzymes. Finally, I discuss the challenges and foreseeable future developments toward a better understanding of the functioning of these complex macromolecules and their exploitation in technological devices. American Chemical Society 2021-01-27 /pmc/articles/PMC7876673/ /pubmed/33585730 http://dx.doi.org/10.1021/acsomega.0c05746 Text en © 2021 The Author. Published by American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Murgida, Daniel H. In Situ Spectroelectrochemical Investigations of Electrode-Confined Electron-Transferring Proteins and Redox Enzymes |
title | In Situ Spectroelectrochemical Investigations of Electrode-Confined
Electron-Transferring Proteins and Redox Enzymes |
title_full | In Situ Spectroelectrochemical Investigations of Electrode-Confined
Electron-Transferring Proteins and Redox Enzymes |
title_fullStr | In Situ Spectroelectrochemical Investigations of Electrode-Confined
Electron-Transferring Proteins and Redox Enzymes |
title_full_unstemmed | In Situ Spectroelectrochemical Investigations of Electrode-Confined
Electron-Transferring Proteins and Redox Enzymes |
title_short | In Situ Spectroelectrochemical Investigations of Electrode-Confined
Electron-Transferring Proteins and Redox Enzymes |
title_sort | in situ spectroelectrochemical investigations of electrode-confined
electron-transferring proteins and redox enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7876673/ https://www.ncbi.nlm.nih.gov/pubmed/33585730 http://dx.doi.org/10.1021/acsomega.0c05746 |
work_keys_str_mv | AT murgidadanielh insituspectroelectrochemicalinvestigationsofelectrodeconfinedelectrontransferringproteinsandredoxenzymes |