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Issue 41, 2010
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Zinc transfer from the embryo-specific metallothionein EC from wheat: a case study

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Abstract

The direct observation of binding and release of spectroscopically silent metal ions such as Zn2+ and Ca2+ by proteins has been challenging before the advent of native electrospray ionisation mass spectrometry. This report highlights the powerful capability of ESI-MS to provide insight into metalloprotein speciation that is independent of any spectroscopic property. Using the zinc-binding plant metallothionein EC from wheat as a study case, we show that ESI-MS is unique amongst other techniques in capturing intermediary metallospecies that evolve during the course of metal transfer to the chelator EDTA, as a model reaction to mimic the biological function of the protein as a zinc donor. Zinc release from the two-domain protein EC appears to be extremely rapid and non-cooperative, and progresses with loss of one zinc ion from the fully loaded Zn6 species, and a transient build-up of Zn5 and Zn4 species, which further react to give species with 0-3 zinc ions bound. 1H NMR data has provided further insights into the different behaviour of the two domains upon metal depletion.

Graphical abstract: Zinc transfer from the embryo-specific metallothionein EC from wheat: a case study

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Publication details

The article was received on 25 May 2010, accepted on 01 Sep 2010 and first published on 27 Sep 2010


Article type: Paper
DOI: 10.1039/C0CP00680G
Phys. Chem. Chem. Phys., 2010,12, 13408-13418

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    Zinc transfer from the embryo-specific metallothionein EC from wheat: a case study

    O. I. Leszczyszyn and C. A. Blindauer, Phys. Chem. Chem. Phys., 2010, 12, 13408
    DOI: 10.1039/C0CP00680G

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