Imperial College London
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DrElenaChekmeneva

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Research Associate - Structural Elucidation
 
 
 
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e.chekmeneva

 
 
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Location

 

Institute of Reproductive and Developmental BiologyHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Chekmeneva:2010:10.1016/j.jelechem.2010.03.021,
author = {Chekmeneva, E and Diaz-Cruz, JM and Arino, C and Esteban, M},
doi = {10.1016/j.jelechem.2010.03.021},
journal = {Journal of Electroanalytical Chemistry},
pages = {20--24},
title = {Binding of Hg2+ by Cys, Cys-Gly and reduced glutathione: Study by differential pulse voltammetry on rotating Au-disk electrode, electrospray ionization mass-spectrometry and isothermal titration calorimetry},
url = {http://dx.doi.org/10.1016/j.jelechem.2010.03.021},
volume = {644},
year = {2010}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The study of Hg2+ binding with short-chain thiols as cysteine (Cys), dipeptide Cys-Gly and reduced glutathione (GSH) was performed by a recently proposed voltammetric method, using the rotating Au-disk electrode. For every thiol a similar complexation pattern was obtained. The highly stable Hg(thiol)(2) complexes are formed with an excess (at least twofold) of the ligand, while at lower ligand-to-Hg ratios the Hg(thiol) species formation is observed. These results were deduced on basis of Multivariate Curve Resolution with Alternating Least Squares (MCR-ALS) data analysis. The electrochemical results were completed with electrospray ionization mass-spectrometry (ESI-MS) experiments that provided the stoichiometries of the complexes. For Cys and Cys-Gly several complexes were detected, depending on the Hg2+-ligand ratio, while for GSH only Hg(GSH) and Hg(GSH)(2) species were observed. Isothermal titration calorimetry (ITC) was used to analyze some thermodynamic characteristic of the interactions between Hg2+ and GSH. This information is valuable because it confirms electroanalytical findings and gives deeper insight into the course of the interactions. (C) 2010 Elsevier B.V. All rights reserved.
AU  - Chekmeneva,E
AU  - Diaz-Cruz,JM
AU  - Arino,C
AU  - Esteban,M
DO  - 10.1016/j.jelechem.2010.03.021
EP  - 24
PY  - 2010///
SN  - 1572-6657
SP  - 20
TI  - Binding of Hg2+ by Cys, Cys-Gly and reduced glutathione: Study by differential pulse voltammetry on rotating Au-disk electrode, electrospray ionization mass-spectrometry and isothermal titration calorimetry
T2  - Journal of Electroanalytical Chemistry
UR  - http://dx.doi.org/10.1016/j.jelechem.2010.03.021
VL  - 644
ER  -
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