ArticleMetallomics : integrated biometal science2023
63Cu(I) binding to human kidney 68Zn7-βα MT1A: determination of Cu(I)-thiolate cluster domain specificity from ESI-MS and room temperature phosphorescence spectroscopy.
Article in Metallomics : integrated biometal science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Oxidative pathways of apo, partially, and fully Zn(II)- and Cd(II)-metalated human metallothionein-3 are dominated by disulfide bond formation.The FEBS journal · 2025Article
- Combining Native Mass Spectrometry and Proteomics to Differentiate and Map the Metalloform Landscape in Metallothioneins.Journal of proteome research · 2024Article
- ESI-MS analysis of Cu(I) binding to apo and Zn7 human metallothionein 1A, 2, and 3 identifies the formation of a similar series of metallated species with no individual isoform optimization for Cu(I).Metallomics : integrated biometal science · 2024Article
- Structural Characterization of Cu(I)/Zn(II)-metallothionein-3 by Ion Mobility Mass Spectrometry and Top-Down Mass Spectrometry.Analytical chemistry · 2023Article
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Abstract
Mammalian metallothioneins (MTs) are important proteins in Zn(II) and Cu(I) homeostasis with the Zn(II) and Cu(I) binding to the 20 cysteines in metal-thiolate clusters. Previous electrospray ionization (ESI) mass spectrometric (MS) analyses of Cu(I) binding to Zn7-MT were complicated by significant overlap of the natural abundance isotopic patterns for Zn(II) and Cu(I) leading to impossibly ambiguous stoichiometries. In this paper, isotopically pure 63Cu(I) and 68Zn(II) allowed determination of the specific stoichiometries in the 68 Zn,63Cu-βα MT1A species formed following the stepwise addition of 63Cu(I) to 68Zn7-βα MT1A. These species were characterized by ESI-MS and room temperature emission spectroscopy. The key species that form and their emission band centres are Zn5Cu5-βα MT1A (λ = 684 nm), Zn4Cu6-βα MT1A (λ = 750 nm), Zn3Cu9-βα MT1A (λ = 750 nm), Zn2Cu10-βα MT1A (λ = 750 nm), and Zn1Cu14-βα MT1A (λ = 634 nm). The specific domain stoichiometry of each species was determined by assessing the species forming following 63Cu(I) addition to the 68Zn3-β MT1A and 68Zn4-α MT1A domain fragments. The domain fragment emission suggests that Zn5Cu5-βα MT1A contains a Zn1Cu5-β cluster and the Zn4Cu6-βα MT1A, Zn3Cu9-βα MT1A, and Zn2Cu10-βα MT1A each contain a Cu6-β cluster. The species forming with >10 mol. eq. of 63Cu(I) in βα-MT1A exhibit emission from the Cu6-β cluster and an α domain cluster. This high emission intensity is seen at the end of the titrations of 68Zn7-βα MT1A and the 68Zn4-α MT1A domain fragment suggesting that the initial presence of the Zn(II) results in clustered Cu(I) binding in the α domain.
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