The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems
Electron paramagnetic resonance (EPR) spectroscopy has emerged as an ideal biophysical tool to study complex biological processes. EPR spectroscopy can follow minor conformational changes in various proteins as a function of ligand or protein binding or interactions with high resolution and sensitiv...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-12-01
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| Series: | Magnetochemistry |
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| Online Access: | https://www.mdpi.com/2312-7481/8/1/3 |
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| author | Shelly Meron Yulia Shenberger Sharon Ruthstein |
| author_facet | Shelly Meron Yulia Shenberger Sharon Ruthstein |
| author_sort | Shelly Meron |
| collection | DOAJ |
| description | Electron paramagnetic resonance (EPR) spectroscopy has emerged as an ideal biophysical tool to study complex biological processes. EPR spectroscopy can follow minor conformational changes in various proteins as a function of ligand or protein binding or interactions with high resolution and sensitivity. Resolving cellular mechanisms, involving small ligand binding or metal ion transfer, is not trivial and cannot be studied using conventional biophysical tools. In recent years, our group has been using EPR spectroscopy to study the mechanism underlying copper ion transfer in eukaryotic and prokaryotic systems. This mini-review focuses on our achievements following copper metal coordination in the diamagnetic oxidation state, Cu(I), between biomolecules. We discuss the conformational changes induced in proteins upon Cu(I) binding, as well as the conformational changes induced in two proteins involved in Cu(I) transfer. We also consider how EPR spectroscopy, together with other biophysical and computational tools, can identify the Cu(I)-binding sites. This work describes the advantages of EPR spectroscopy for studying biological processes that involve small ligand binding and transfer between intracellular proteins. |
| first_indexed | 2024-03-10T01:05:55Z |
| format | Article |
| id | doaj.art-e3b20d6c103e46ca810327e5ce4fc84a |
| institution | Directory Open Access Journal |
| issn | 2312-7481 |
| language | English |
| last_indexed | 2024-03-10T01:05:55Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Magnetochemistry |
| spelling | doaj.art-e3b20d6c103e46ca810327e5ce4fc84a2023-11-23T14:27:02ZengMDPI AGMagnetochemistry2312-74812021-12-0181310.3390/magnetochemistry8010003The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological SystemsShelly Meron0Yulia Shenberger1Sharon Ruthstein2Department of Chemistry and the Institute of Nanotechnology and Advanced Materials (BINA), Bar-Ilan University, Ramat-Gan 5290002, IsraelDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials (BINA), Bar-Ilan University, Ramat-Gan 5290002, IsraelDepartment of Chemistry and the Institute of Nanotechnology and Advanced Materials (BINA), Bar-Ilan University, Ramat-Gan 5290002, IsraelElectron paramagnetic resonance (EPR) spectroscopy has emerged as an ideal biophysical tool to study complex biological processes. EPR spectroscopy can follow minor conformational changes in various proteins as a function of ligand or protein binding or interactions with high resolution and sensitivity. Resolving cellular mechanisms, involving small ligand binding or metal ion transfer, is not trivial and cannot be studied using conventional biophysical tools. In recent years, our group has been using EPR spectroscopy to study the mechanism underlying copper ion transfer in eukaryotic and prokaryotic systems. This mini-review focuses on our achievements following copper metal coordination in the diamagnetic oxidation state, Cu(I), between biomolecules. We discuss the conformational changes induced in proteins upon Cu(I) binding, as well as the conformational changes induced in two proteins involved in Cu(I) transfer. We also consider how EPR spectroscopy, together with other biophysical and computational tools, can identify the Cu(I)-binding sites. This work describes the advantages of EPR spectroscopy for studying biological processes that involve small ligand binding and transfer between intracellular proteins.https://www.mdpi.com/2312-7481/8/1/3copper cyclecopper metabolismCW-EPRDEEREPR spectroscopy |
| spellingShingle | Shelly Meron Yulia Shenberger Sharon Ruthstein The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems Magnetochemistry copper cycle copper metabolism CW-EPR DEER EPR spectroscopy |
| title | The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems |
| title_full | The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems |
| title_fullStr | The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems |
| title_full_unstemmed | The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems |
| title_short | The Advantages of EPR Spectroscopy in Exploring Diamagnetic Metal Ion Binding and Transfer Mechanisms in Biological Systems |
| title_sort | advantages of epr spectroscopy in exploring diamagnetic metal ion binding and transfer mechanisms in biological systems |
| topic | copper cycle copper metabolism CW-EPR DEER EPR spectroscopy |
| url | https://www.mdpi.com/2312-7481/8/1/3 |
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