Ag⁺ Ion Binding to Human Metallothionein-2A Is Cooperative and Domain Specific.

ABSTRACT: Metallothioneins (MTs) constitute a family of cysteine-rich proteins that play key biological roles for a wide range of metal ions, but unlike many other metalloproteins, the structures of apo- and partially metalated MTs are not well understood. Here, we combine nano-electrospray ionization-mass spectrometry (ESI-MS) and nano-ESI-ion mobility (IM)-MS with collision-induced unfolding (CIU), chemical labeling using N-ethylmaleimide (NEM), and both bottom-up and top-down proteomics in an effort to better understand the metal binding sites of the partially metalated forms of human MT-2A, viz., Ag₄-MT. The results for Ag₄-MT are then compared to similar results obtained for Cd₄-MT. The results show that Ag₄-MT is a cooperative product, and dat

SUBMITTER: Dong S 

PROVIDER: S-EPMC8114364 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature