Correlation of acid–base chemistry of phytochelatin PC2 with its coordination properties towards the toxic metal ion Cd(<scp>ii</scp>)

Dorčák, Vlastimil; Krężel, Artur

doi:10.1039/b301357j

Cited by 53 publications

(47 citation statements)

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“…As the complexity of the mass spectra was high, they were analyzed in four steps, by establishing:The charge of the ionThe number of cadmium ions attached to thiopeptide by checking the agreement between the theoretical and the experimental isotopic profileThe number of hydrogen molecules lost during cadmium binding (one H 2 per Cd ion [18]) or oxidation of peptideThe agreement between the signals observed in positive and negative ion modes…”

Section: Resultsmentioning

confidence: 99%

“…However, the proposed stoichiometry was limited to LMW complexes such as Cd 1 L 1 and Cd 1 L 2 for GSH and PC 2 , and Cd 1 L 1 , Cd 2 L 1 , and Cd 3 L 1 for PC 2 , PC 3 , and PC 4 . Other approaches used were also limited to LMW cadmium complexes of GSH and PCs, such as potentiometric pH titration [16], UV spectroscopy [17], NMR spectroscopy [18], and differential pulse voltammetry/polarography [15, 16, 19]. …”

Section: Introductionmentioning

confidence: 99%

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SEC ICP MS and CZE ICP MS investigation of medium and high molecular weight complexes formed by cadmium ions with phytochelatins

et al. 2013

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Size-exclusion chromatography (SEC) and capillary zone electrophoresis (CZE) coupled with inductively coupled plasma mass spectrometry were applied to characterize low, medium, and high molecular weight cadmium complexes with glutathione and phytochelatins (PCs). The dominant stoichiometry of the complexes formed in vitro was established as 1:1 using electrospray ionization mass spectrometry. Calculated molecular masses of Cd1L1 complexes were used for calibration of the SEC and CZE methods. The results showed a lower (2 kDa) SEC column exclusion limit for cadmium complexes compared with free peptides (10 kDa), and most of the high molecular weight cadmium species were eluted in the void volume of the column. Moreover, the CZE method based on the semiempirical model of Offord to elucidate peptide migration allowed us to show a high propensity of Cd–PC complexes for polymorphism on complexation, which was also observed for extracts of Arabidopsis thaliana treated with cadmium. All the information presented is vital for understanding the mechanism of metal deactivation in plants.FigureEstimation of molecular mass of Cd-thiopeptide complexes by size electrophoretic mobilityElectronic supplementary materialThe online version of this article (doi:10.1007/s00216-013-6868-3) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

SEC ICP MS and CZE ICP MS investigation of medium and high molecular weight complexes formed by cadmium ions with phytochelatins

et al. 2013

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“…The exact difference in acidity of the sulphur binding ligands cannot be observed in UV-titrations due to the presence of 20 cysteines and overlapping dissociation events (macroscopic vs microscopic p K a ) [85,86]. …”

Section: Zn2+ Affinity For Human Metallothioneinmentioning

confidence: 99%

The Functions of Metamorphic Metallothioneins in Zinc and Copper Metabolism

Krężel

Maret

2017

IJMS

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223

143

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Recent discoveries in zinc biology provide a new platform for discussing the primary physiological functions of mammalian metallothioneins (MTs) and their exquisite zinc-dependent regulation. It is now understood that the control of cellular zinc homeostasis includes buffering of Zn2+ ions at picomolar concentrations, extensive subcellular re-distribution of Zn2+, the loading of exocytotic vesicles with zinc species, and the control of Zn2+ ion signalling. In parallel, characteristic features of human MTs became known: their graded affinities for Zn2+ and the redox activity of their thiolate coordination environments. Unlike the single species that structural models of mammalian MTs describe with a set of seven divalent or eight to twelve monovalent metal ions, MTs are metamorphic. In vivo, they exist as many species differing in redox state and load with different metal ions. The functions of mammalian MTs should no longer be considered elusive or enigmatic because it is now evident that the reactivity and coordination dynamics of MTs with Zn2+ and Cu+ match the biological requirements for controlling—binding and delivering—these cellular metal ions, thus completing a 60-year search for their functions. MT represents a unique biological principle for buffering the most competitive essential metal ions Zn2+ and Cu+. How this knowledge translates to the function of other families of MTs awaits further insights into the specifics of how their properties relate to zinc and copper metabolism in other organisms.

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“…The reagent excess, cleavage and purification were performed essentially as previously described [55][56][57]. The peptides were acetylated on the N-terminus using acetic anhydride in the presence of DIEA and cleaved from the resin with a mixture of TFA/ thioanisole/EDT/anisol (90/5/3/2 v/v/v/v) over a period of 2 h followed by precipitation in cold (− 20°C) diethyl ether.…”

Section: Peptide Synthesismentioning

confidence: 99%

Molar absorption coefficients and stability constants of metal complexes of 4-(2-pyridylazo)resorcinol (PAR): Revisiting common chelating probe for the study of metalloproteins

Kocyła

Pomorski

Krężel

2015

Journal of Inorganic Biochemistry

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Correlation of acid–base chemistry of phytochelatin PC2 with its coordination properties towards the toxic metal ion Cd(ii)

Cited by 53 publications

References 45 publications

SEC ICP MS and CZE ICP MS investigation of medium and high molecular weight complexes formed by cadmium ions with phytochelatins

SEC ICP MS and CZE ICP MS investigation of medium and high molecular weight complexes formed by cadmium ions with phytochelatins

The Functions of Metamorphic Metallothioneins in Zinc and Copper Metabolism

Molar absorption coefficients and stability constants of metal complexes of 4-(2-pyridylazo)resorcinol (PAR): Revisiting common chelating probe for the study of metalloproteins

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