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• W2007440111 abstract "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." @default.
• W2007440111 created "2016-06-24" @default.
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• W2007440111 date "2010-05-01" @default.
• W2007440111 modified "2023-10-17" @default.
• W2007440111 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" @default.
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• W2007440111 doi "https://doi.org/10.1016/j.jelechem.2010.03.021" @default.
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