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PERIS DÍAZ, M D. -- RICHTERA, L. -- ZÍTKA, O. -- KRĘŻEL, A. -- ADAM, V. A chemometric-assisted voltammetric analysis of free and Zn(II)-loaded metallothionein-3 states. Bioelectrochemistry. 2020. v. 134, no. August, ISSN 1567-5394. URL: https://doi.org/10.1016/j.bioelechem.2020.107501

Original name: A chemometric-assisted voltammetric analysis of free and Zn(II)-loaded metallothionein-3 states
Czech name:
Written by (author):
Department:
Department of Chemistry and Biochemistry
Kind of publication:
article in a professional periodical
Periodical: Bioelectrochemistry
Nature of article:
paper
Volume no. (year):
134
Periodical number within the volume:
August
Year of publication: 2020
Starting page:
Up to page:
Number of pages:
8
Sub-specification: článek je obsažen v databázi Web of Science
UT code by Web of Science:
EID code by Scopus:
Form of publication: printed version
Original language:
English
Description in original language:
We focused on the application of mass spectrometry and electrochemical methods combined with a chemometric analysis for the characterization of partially metallothionein-3 species. The results showed decreased Cat1 and Cat2 signals for the Zn(II)-loaded MT3 species with respect to the metal-free protein, which might be explained by the arrangement of tetrahedral metal-thiolate coordination environments and the formation of metal clusters. Moreover, there was a decrease in the Cat1 and Cat2 signals, and a plateau was reached with 4-5 Zn(II) ions that corresponded to the formation of the C-terminal α-domain. Regarding the Zn7-xMT3 complexes, we observed three different electrochemical behaviours for the Zn1-2MT3, Zn3-6MT3 and Zn7MT3 species. The difference for Zn1-2MT3 might be explained by the formation of independent ZnS4 cores in this stage that differ with respect to the formation of ZnxCysy clusters with an increased Zn(II) loading. The binding of the third Zn(II) ion to MT3 resulted in high sample heterogeneity due the co-existence of Zn3-6MT3. Finally, the Zn7MT3 protein showed a third type of behaviour. The fact that there were no free Cys residues might explain this phenomenon. Thus, this research identifies the major proteins responsible for zinc buffering in the cell.
Description in English:
Description in Czech:
Year of submission:
2020
Year of transmission:
RIV identification number:
URL:
https://doi.org/10.1016/j.bioelechem.2020.107501
 
Entry made by:
Last change:
04/03/2020 11:54 (Markéta Hejčová, DiS.)

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Source specification:

Bioelectrochemistry. ISSN 1567-5394.

Original name:
Bioelectrochemistry
English name:
Czech name:
Written by (author):
Kind of publication:
magazine
ISSN:
1567-5394
Country of publisher: Kingdom of the Netherlands
Place of publishing:
Publisher:
Elsevier Science SA
URL:
Reviewed magazine: no
Original language:
Description in original language:
Description in English:
Description in Czech:
 
Entry made by: Lenka Baláková
Last change:
03/14/2012 20:39 (Ing. Aleš Kutín)

Evaluation of publication:

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