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Related Concept Videos

Metal-Ligand Bonds02:51

Metal-Ligand Bonds

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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Extraction: Advanced Methods00:56

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Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is...
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Complexation Equilibria: The Chelate Effect01:19

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In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
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In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
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Sulfur Assimilation01:20

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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
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Related Experiment Video

Updated: Apr 20, 2026

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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Metallothionein-protein interactions.

Sílvia Atrian, Mercè Capdevila

    Biomolecular Concepts
    |December 2, 2014
    PubMed
    Summary

    Metallothioneins (MTs) are versatile proteins involved in metal ion regulation and stress responses. This review details their interactions with various proteins, impacting neurodegeneration, metabolism, and cancer.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Metallothioneins (MTs) are cysteine-rich proteins crucial for metal ion homeostasis and cellular protection.
    • MTs participate in detoxification, stress responses, and various pathological processes, including neurodegeneration and cancer.

    Purpose of the Study:

    • To comprehensively review intracellular and extracellular interactions of MTs with other proteins.
    • To highlight the role of MTs in regulating metal ion homeostasis and cellular functions.
    • To discuss the implications of MT-protein interactions for biomedical applications.

    Main Methods:

    • Literature review of existing studies on MT-protein interactions.
    • Analysis of reported physical interactions and metal exchange reactions.

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  • Examination of MTs' roles in different physiological and pathological contexts.

    • Main Results:

    • MTs interact with kidney receptors (megalin) and transporters (transthyretin).
    • Significant interactions occur in the central nervous system, involving neuronal secretion and metal ion control in neurodegenerative disease-associated peptides (Aβ, α-synuclein, prions).
    • MTs regulate zinc-dependent enzymes and transcription factors, influencing metabolism, gene expression, cell cycle, and oncogenesis.

    Conclusions:

    • MT-protein interactions are critical for diverse cellular functions, from metal homeostasis to regulating gene expression and cell proliferation.
    • Understanding these interactions offers potential for novel therapeutic strategies in neurodegenerative diseases, cancer, and other pathologies.
    • Further research into MT interactions, particularly non-mammalian systems, could reveal new biomedical applications.