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EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms

[Image: see text] In the last 20 years, the use of electron paramagnetic resonance (EPR) has made a pronounced and lasting impact in the field of structural biology. The advantage of EPR spectroscopy over other structural techniques is its ability to target even minor conformational changes in any b...

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Autores principales: Hofmann, Lukas, Ruthstein, Sharon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9549461/
https://www.ncbi.nlm.nih.gov/pubmed/36137278
http://dx.doi.org/10.1021/acs.jpcb.2c05235
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author Hofmann, Lukas
Ruthstein, Sharon
author_facet Hofmann, Lukas
Ruthstein, Sharon
author_sort Hofmann, Lukas
collection PubMed
description [Image: see text] In the last 20 years, the use of electron paramagnetic resonance (EPR) has made a pronounced and lasting impact in the field of structural biology. The advantage of EPR spectroscopy over other structural techniques is its ability to target even minor conformational changes in any biomolecule or macromolecular complex, independent of its size or complexity, or whether it is in solution or in the cell during a biological or chemical reaction. Here, we focus on the use of EPR spectroscopy to study transmembrane transport and transcription mechanisms. We discuss experimental and analytical concerns when referring to studies of two biological reaction mechanisms, namely, transfer of copper ions by the human copper transporter hCtr1 and the mechanism of action of the Escherichia coli copper-dependent transcription factor CueR. Last, we elaborate on future avenues in the field of EPR structural biology.
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spelling pubmed-95494612022-10-11 EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms Hofmann, Lukas Ruthstein, Sharon J Phys Chem B [Image: see text] In the last 20 years, the use of electron paramagnetic resonance (EPR) has made a pronounced and lasting impact in the field of structural biology. The advantage of EPR spectroscopy over other structural techniques is its ability to target even minor conformational changes in any biomolecule or macromolecular complex, independent of its size or complexity, or whether it is in solution or in the cell during a biological or chemical reaction. Here, we focus on the use of EPR spectroscopy to study transmembrane transport and transcription mechanisms. We discuss experimental and analytical concerns when referring to studies of two biological reaction mechanisms, namely, transfer of copper ions by the human copper transporter hCtr1 and the mechanism of action of the Escherichia coli copper-dependent transcription factor CueR. Last, we elaborate on future avenues in the field of EPR structural biology. American Chemical Society 2022-09-22 2022-10-06 /pmc/articles/PMC9549461/ /pubmed/36137278 http://dx.doi.org/10.1021/acs.jpcb.2c05235 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Hofmann, Lukas
Ruthstein, Sharon
EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms
title EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms
title_full EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms
title_fullStr EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms
title_full_unstemmed EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms
title_short EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms
title_sort epr spectroscopy provides new insights into complex biological reaction mechanisms
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9549461/
https://www.ncbi.nlm.nih.gov/pubmed/36137278
http://dx.doi.org/10.1021/acs.jpcb.2c05235
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