Acute Toxicity of Divalent Mercury to Bacteria Explained by the Formation of Dicysteinate and Tetracysteinate Complexes Bound to Proteins in Escherichia coli and Bacillus subtilis-Reference-Cited by-同舟云学术

Acute Toxicity of Divalent Mercury to Bacteria Explained by the Formation of Dicysteinate and Tetracysteinate Complexes Bound to Proteins in Escherichia coli and Bacillus subtilis

Published:2021-02-25 Issue:6 Volume:55 Page:3612-3623
ISSN:0013-936X
Container-title:Environmental Science & Technology
language:en
Short-container-title:Environ. Sci. Technol.

Author:

Manceau Alain¹^ORCID,Nagy Kathryn L.²^ORCID,Glatzel Pieter³^ORCID,Bourdineaud Jean-Paul⁴

Affiliation:

1. Université Grenoble Alpes, CNRS, ISTerre, CS 40700, 38058 Grenoble, France

2. Department of Earth and Environmental Sciences, University of Illinois at Chicago, MC-186, 845 West Taylor Street, Chicago, Illinois 60607, United States

3. European Synchrotron Radiation Facility (ESRF), 71 Rue des Martyrs, 38000 Grenoble, France

4. Institut Européen de Chimie et Biologie, Université de Bordeaux, CNRS, UMR 5234, 2 rue Escarpit, 33607 Pessac, France

Funder

Agence Nationale de la Recherche

Division of Earth Sciences

Publisher

American Chemical Society (ACS)

Subject

Environmental Chemistry,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.est.0c05202

Reference105 articles.

1. Bacterial mercury resistance from atoms to ecosystems

2. Mercury-199 NMR of the Metal Receptor Site in MerR and Its Protein-DNA Complex

3. A Mercuric Ion Uptake Role for the Integral Inner Membrane Protein, MerC, Involved in Bacterial Mercuric Ion Resistance

4. Structures of the Reduced and Mercury-Bound Forms of MerP, the Periplasmic Protein from the Bacterial Mercury Detoxification System,

5. MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?

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