Thomas, SA, Mishra, B and Myneni, SCB (2019) High Energy Resolution-X-ray Absorption Near Edge Structure Spectroscopy Reveals Zn Ligation in Whole Cell Bacteria. Journal of Physical Chemistry Letters, 10. pp. 2585-2592. ISSN 1948-7185
Abstract
Identifying the zinc (Zn) ligation and coordination environment in complex biological and environmental systems is crucial to understand the role of Zn as a biologically essential but sometimes toxic metal. Most studies on Zn coordination in biological or environmental samples rely on the extended X-ray absorption fine structure (EXAFS) region of a Zn K-edge X-ray absorption spectroscopy (XAS) spectrum. However, EXAFS analysis cannot identify unique nearest neighbors with similar atomic number (i.e., O versus N) and provides little information on Zn ligation. Herein, we demonstrate that high energy-resolution X-ray absorption near edge structure (HR-XANES) spectroscopy enables the direct determination of Zn ligation in whole cell bacteria, providing additional insights lost from EXAFS analysis at a fraction of the scan time and Zn concentration. HR-XANES is a relatively new technique that has improved our understanding of trace metals (e.g., Hg, Cu, and Ce) in dilute systems. This study is the first to show that HR-XANES can unambiguously detect Zn coordination to carboxyl, phosphoryl, imidazole, and/or thiol moieties in model microorganisms.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Copyright © 2019 American Chemical Society. This document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Journal of Physical Chemistry Letters after peer review. To access the final edited and published work see http://doi.org/10.1021/acs.jpclett.9b01186. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemical & Process Engineering (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 08 May 2019 14:15 |
Last Modified: | 30 Apr 2020 00:38 |
Status: | Published |
Publisher: | American Chemical Society |
Identification Number: | 10.1021/acs.jpclett.9b01186 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:145761 |