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Related Concept Videos

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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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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Protein metalation in biology.

Andrew W Foster1, Tessa R Young1, Peter T Chivers1

  • 1Department of Biosciences, Durham University, Durham, DH1 3LE, UK; Department of Chemistry, Durham University, Durham, DH1 3LE, UK.

Current Opinion in Chemical Biology
|November 11, 2021
PubMed
Summary

Biological metalation involves proteins competing for limited metals, unlike lab conditions. Understanding cellular metal homeostasis reveals how cells maintain optimal metal levels for protein function.

Keywords:
CobaltCopperIronMagnesiumManganeseMetal availabilityMetal sensorsMetal specificityMetalation calculatorNickelZinc

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Area of Science:

  • Biochemistry
  • Metallomics
  • Cell Biology

Background:

  • Inorganic metals are essential for protein function, but their cellular availability is tightly regulated.
  • Protein metalation, the process of incorporating metals into proteins, is crucial for biological activity.
  • Extracellular conditions often involve metal excess, contrasting with intracellular metal scarcity.

Purpose of the Study:

  • To summarize mechanisms of metal homeostasis in biological systems.
  • To elucidate how cells maintain optimal metal concentrations for protein metalation.
  • To compare intracellular metal binding dynamics with extracellular conditions.

Main Methods:

  • Review of existing literature on metal homeostasis.
  • Analysis of metal-binding affinities in cellular environments.
  • Comparison of metal-protein binding strengths versus competing cellular sites.

Main Results:

  • Biological systems employ sophisticated metal homeostasis mechanisms to manage metal availability.
  • Cells prioritize specific metal-binding sites, competing for limited metal ions.
  • The strength of metal binding to proteins is balanced against binding to other cellular components.

Conclusions:

  • Cellular metal homeostasis ensures sufficient metal supply for essential proteins.
  • Understanding metal binding affinities is key to comprehending protein metalation in vivo.
  • This research highlights the intricate strategies cells use to acquire and utilize metals.