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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...
Crystal Field Theory - Octahedral Complexes02:58

Crystal Field Theory - Octahedral Complexes

Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Complexation Equilibria: Overview01:23

Complexation Equilibria: Overview

Complexation reactions take place when dative or coordinate covalent bonds form between metal ions and ligands. The compounds formed in these reactions are called coordination compounds. The number of bonds formed between the metal ion and the ligands is called its coordination number. Generally, most metal ions in an aqueous solution are solvated by water molecules and thus exist as aqua complexes.
The equilibrium constant of the complexation reaction is represented as the formation constant...

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

Published on: September 7, 2019

Structural transitions in ion coordination driven by changes in competition for ligand binding.

Sameer Varma1, Susan B Rempe

  • 1Sandia National Laboratories, Albuquerque, New Mexico 87185, USA. svarma@sandia.gov

Journal of the American Chemical Society
|October 29, 2008
PubMed
Summary

Understanding ion partitioning requires considering solvation effects. Reducing free energy penalties for ligand extraction stabilizes higher ion coordination, crucial for biomolecular interactions and ion binding.

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

Published on: December 16, 2013

Area of Science:

  • Biophysical Chemistry
  • Computational Chemistry
  • Structural Biology

Background:

  • Sodium (Na+) and potassium (K+) ions in water adopt specific coordination states.
  • Ions often transition to states with higher coordination numbers in biological systems, despite an apparent free energy cost.

Purpose of the Study:

  • To elucidate the role of the solvation environment in driving ion coordination structure transitions.
  • To understand the energetic factors governing ion partitioning into higher coordination states.

Main Methods:

  • Statistical theory of solutions
  • Quantum chemical simulations
  • Classical mechanics simulations
  • Structural informatics

Main Results:

  • The solvation environment significantly influences ion coordination transitions.
  • Free energy penalties for ligand extraction from solvation shells impact ion coordination preferences.
  • Lowering these penalties enhances stability of higher-order ion coordinations and reduces partitioning costs.
  • Reduced favorable interactions of ligands with non-ion atoms decrease penalties and increase coordination preferences.

Conclusions:

  • Solvation phase properties are key drivers of ion coordination structure transitions.
  • Modulating ligand-environment interactions can alter ion coordination preferences, mimicking Hofmeister effects.
  • Findings are applicable to other ions and influenced by ligand density, chemistry, and temperature.