Mobility of Copper in Binding Sites in Rabbit Liver Metallothionein 2

Green, Anna Rae; Stillman, Martin J.

doi:10.1021/ic950540a

Cited by 20 publications

(5 citation statements)

References 48 publications

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“…The relatively high compactness protected the metal ions from the solvent intrusion. All of these findings were consistent with the previous research reports (Green and Stillman ; Vergani and others ).…”

Section: Resultssupporting

confidence: 93%

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe²⁺ Complex: The Role of Metallothionein

Zhang

Fang

et al. 2017

Journal of Food Science

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Metallothionein (MT) is a low-molecular-weight protein with high metal-ion affinity. If the intracellular concentrations of metals are too high or if toxic metals are present within the cell, then the synthesis of MTs is induced and generated. In our previous work, it was found that the prepared hydrolysate-metal element complex showed obvious depuration activity of heavy metals (Cd ) from blue mussel (Mytilus edulis). This study provided further the depuration mechanisms of Cd from mussel (M. edulis), in particular to the role of MT and its chelate during the depuration process.

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Section: Resultssupporting

confidence: 93%

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe²⁺ Complex: The Role of Metallothionein

Zhang

Fang

et al. 2017

Journal of Food Science

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“…The temperature dependence of the luminescence properties of Cu(I) MT-2, coupled with examination of the CD spectra, revealed information on the modes of binding of Cu(I) to MT-2 . It was found that the α domain emitted much more intensely than its β counterpart in MT-2.…”

Section: B Copper(i) In Metallothionein Proteinsmentioning

confidence: 99%

Photoluminescence Properties of Multinuclear Copper(I) Compounds

1999

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ContentsI. Introduction 3625 II. Tetranuclear Cuprous Halide Clusters 3626 A. Cu 4 I 4 Clusters 3627 B. Other Cu 4 X 4 Clusters 3631 C. Rigidochromic Effects 3632 D. Excited State Energy and Electron Transfer 3633 E. Cu 4 X 4 (phosphines) 4 3635 III. Other Cuprous Halide Complexes 3635 IV. Polynuclear Cu(I) and Ag(I) Complexes with Chalcogen Ligands 3636 A. Dynamic Quenching Studies. 3639 B. Copper(I) in Metallothionein Proteins. 3639 V. Cuprous Clusters with Acetylide Ligands 3640 VI. Other Cuprous Polynuclear Systems 3642 VII. Gold(I) Complexes 3645 VIII. Overview and Summary 3645 IX. Acknowledgments 3646 X. List of Abbreviations 3646 A. Ligands 3646 B. Excited-State Labels Used 3646 XI. References 3646

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“…22,100 Experimental evidence directly disputes this last requirement, as displacement of Zn 2+ from Zn 7 -MT by Cu + occurs in a distributive manner (binding to both domains) followed by a time-and temperature-dependent rearrangement leading to the expected metal ion selectivity. 132,133 It is possible that MT is able to achieve metal ion equilibrium through both the bead-model structure mechanism and through these supermetallated states. Briefly the coordination of an exogenous metal ion to Zn 7 -MT, such as Cd 2+ or Cu + , leads to the transient formation of a (Cd or Cu) 1 Zn 7 -MT followed by a rearrangement and subsequent expulsion of one of the previously bound Zn 2+ ions to form (Cd or Cu) 1 Zn 6 -MT with the expected metal ion specificity.…”

Section: Single Domains: Supermetallation Of Mtmentioning

confidence: 99%

Challenging conventional wisdom: single domain metallothioneins

Sutherland

Stillman

2014

Metallomics

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Metallothioneins (MT) are a family of small cysteine rich proteins that have been implicated in a range of roles including toxic metal detoxification, protection against oxidative stress, and as metallochaperones are undoubtedly involved in the homeostasis of both essential zinc and copper. While complete details of all possible cellular functions are still unknown, it is clear that they must be directly related to both the accessibility and the metal-binding properties of the many cysteine residues in the protein. The most well studied MTs are of mammalian origin and consist of two domains: a β-domain with 9 cysteine residues that sequesters 3 Cd(2+), 3 Zn(2+) or 6 Cu(+) ions, and an α-domain with 11 cysteine residues that sequesters 4 Cd(2+), 4 Zn(2+) or 6 Cu(+) ions. The key to understanding the cellular importance of MT in these different roles is in a precise description of the metallation status before and during reactions. An assessment of all possible and all biologically accessible metallation states is necessary before the functional mechanistic details can be fully determined. Conventionally, it has been considered that metal ions bind in a domain-specific and, therefore, cooperative manner, where the apparently isolated domains fill with their full complement of metal ions immediately with no discernible or measurable intermediates. A number of detailed mechanistic studies of the metallation reactions of mammalian MTs have provided significant insight into the metallation reactions. Recent results from electrospray ionization mass spectrometric studies of the stepwise metallation of the two fragments and the whole protein with Zn(2+), Cd(2+), As(3+) and Bi(3+) indicate a noncooperative mechanism of a declining series of K(F)'s. Of particular note are new details about the early stages of the stepwise metallation reactions, specifically the stability of partially metallated species for As(3+), Cd(2+), and Zn(2+) that do not correspond to the two-domain model. In addition, at the other end of the coordination spectrum are the supermetallated species of MT, where supermetallation defines metallation in excess of traditional levels. It has been reported that with metal ion excess the formation of a single 'super domain' is possible and again this deviates from the two-domain model of MT. In both cases, these results suggest that the structural view of mammalian MT that is of two essentially isolated domains may be the exceptional case and that under the normal conditions of cellular metal-ion concentrations the two domain structure might coexist in equilibrium with various single domain, multi-metal site structures. This review specifically focuses on providing context for these recent studies and the new ideas concerning metallation prior to the establishment of domain-based clusters that these studies suggest.

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Mobility of Copper in Binding Sites in Rabbit Liver Metallothionein 2

Cited by 20 publications

References 48 publications

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe²⁺ Complex: The Role of Metallothionein

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe²⁺ Complex: The Role of Metallothionein

Photoluminescence Properties of Multinuclear Copper(I) Compounds

Challenging conventional wisdom: single domain metallothioneins

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Mobility of Copper in Binding Sites in Rabbit Liver Metallothionein 2

Cited by 20 publications

References 48 publications

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe2+ Complex: The Role of Metallothionein

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe2+ Complex: The Role of Metallothionein

Photoluminescence Properties of Multinuclear Copper(I) Compounds

Challenging conventional wisdom: single domain metallothioneins

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Product

Resources

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Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe²⁺ Complex: The Role of Metallothionein

Depuration of Cadmium from Blue Mussel (Mytilus edulis) by Protein Hydrolysate–Fe²⁺ Complex: The Role of Metallothionein