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Related Concept Videos

Metal-Ligand Bonds02:51

Metal-Ligand Bonds

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...
Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

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...
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Formation of Complex Ions03:45

Formation of Complex Ions

A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...

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Updated: Jun 18, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

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

Published on: December 16, 2013

Supramolecular interactions between functional metal complexes and proteins.

Catherine L Davies1, Emma L Dux, Anne-K Duhme-Klair

  • 1Department of Chemistry, University of York, York, YO10 5DD, UK.

Dalton Transactions (Cambridge, England : 2003)
|November 19, 2009
PubMed
Summary
This summary is machine-generated.

This perspective explores how transition metal complexes bind to proteins through molecular recognition. Applications include artificial enzymes, protein labeling, and drug design, enhancing biological and catalytic functions.

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Area of Science:

  • Bioinorganic Chemistry
  • Chemical Biology
  • Molecular Recognition

Background:

  • Non-covalent interactions and complementarity are crucial for molecular binding.
  • Biological systems like bacterial iron uptake proteins and myoglobin utilize non-covalent forces for metal complex binding.

Purpose of the Study:

  • To illustrate principles and applications of molecular recognition-directed binding of transition metal complexes to proteins.
  • To explore the creation of artificial metalloenzymes with novel catalytic properties.
  • To describe spectroscopic probes for protein investigation and drug design scaffolds.

Main Methods:

  • Review of non-covalent interactions in biological systems.
  • Discussion of native vs. non-native metal centers in artificial metalloenzymes.
  • Examples of spectroscopic probes and drug design strategies.

Main Results:

  • Metal complexes can be directed to bind proteins via molecular recognition.
  • Artificial metalloenzymes can be engineered for new catalytic functions.
  • Metal complexes serve as effective tools for protein labeling, visualization, and drug development.

Conclusions:

  • Molecular recognition offers a powerful strategy for controlling metal complex-protein interactions.
  • This approach enables the development of novel catalysts, diagnostic tools, and therapeutics.
  • The field holds significant potential for advancing chemical biology and medicine.