Metallothioneins (MTs) are metal-binding proteins with low molecular weight and conservative cysteine residues. Metallothionein-4 (MT-4), one of MT isoforms, is first reported to be distributed in a tissue-specific manner, mainly in stratified squamous epithelia. Here, we compare the properties of metal–thiolate clusters in MT-4 to those in MT-1 and MT-3, including the stabilities toward both pH change and EDTA, as well as the exposure of thiolates to solvent. The metal–thiolate clusters in MT-3 show different property and activity to the reactions compared with MT-4 and MT-1. The structure of metal–thiolate clusters in MT-4 is similar to that of MT-1 from the UV and CD spectra. During pH titration and DTNB reaction, MT-4 and MT-1 exhibit comparable behavior. But while reacting with EDTA, the metal–thiolate clusters in MT-4 are more stable than those of MT-1. We suppose the negative charge of the β-domain of MT-4 prevents the EDTA attack to MT-4.
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Abbreviations
- CD:
-
Circular dichroism
- DTNB:
-
5,5′-dithiobis-2-nitrobenzoic acid
- EDTA:
-
Ethylenediamine tetraacetic acid
- ESI-MS:
-
Electrospray ionization-mass spectroscopy
- GST:
-
glutathione sulfur transferase
- LMCT:
-
Ligand metal charge transfer
- MT4:
-
metallothionein-4
- UV–Vis:
-
Ultraviolet visible
- ZT:
-
zinc-transport proteins.
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Cai, B., Zheng, Q. & Huang, ZX. The Properties of the Metal–Thiolate Clusters in Recombinant Mouse Metallothionein-4. Protein J 24, 327–336 (2005). https://doi.org/10.1007/s10930-005-7588-0
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DOI: https://doi.org/10.1007/s10930-005-7588-0