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Related Concept Videos

Valence Bond Theory02:42

Valence Bond Theory

Coordination compounds and complexes exhibit different colors, geometries, and magnetic behavior, depending on the metal atom/ion and ligands from which they are composed. In an attempt to explain the bonding and structure of coordination complexes, Linus Pauling proposed the valence bond theory, or VBT, using the concepts of hybridization and the overlapping of the atomic orbitals. According to VBT, the central metal atom or ion (Lewis acid) hybridizes to provide empty orbitals of suitable...
Colors and Magnetism03:02

Colors and Magnetism

Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human eye.
Structural Isomerism02:34

Structural Isomerism

Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can be...
Structure of Amines01:19

Structure of Amines

The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’ carbon–carbon bond (154 pm). These aspects are illustrated in Figure...
Electron Paramagnetic Resonance (EPR) Spectroscopy: Organic Radicals01:17

Electron Paramagnetic Resonance (EPR) Spectroscopy: Organic Radicals

Ideally, an unpaired electron shows a single peak in the EPR spectrum due to the transition between the two spin energy states. However, coupling interactions can occur between the spins of the unpaired electron and any neighboring spin-active nuclei. This hyperfine coupling results in hyperfine splitting, where the EPR signal is split into multiplets. The signals split into 2nI + 1 peaks, where n is the number of equivalent nuclei and I is the nuclear spin. These splitting patterns provide...
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...

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Related Experiment Video

Updated: May 8, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Human anamorsin binds [2Fe-2S] clusters with unique electronic properties.

Lucia Banci1, Simone Ciofi-Baffoni, Maciej Mikolajczyk

  • 1Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy, banci@cerm.unifi.it.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|August 31, 2013
PubMed
Summary

Human anamorsin protein binds iron-sulfur clusters in two distinct ways. Only one cluster is essential for electron transfer in cytosolic iron-sulfur protein biogenesis.

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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
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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

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioinorganic Chemistry

Background:

  • The anamorsin protein family, including the CIAPIN1 domain, is implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis.
  • This domain contains two cysteine-rich motifs (CX8CX2CXC and CX2CX7CX2C) with poorly defined Fe/S binding and electronic properties.

Purpose of the Study:

  • To elucidate the Fe/S binding capabilities and electronic structures of the cysteine-rich motifs within human anamorsin.
  • To determine the functional role of these motifs in the context of electron transfer and Fe/S protein biogenesis.

Main Methods:

  • Spectroscopic analysis of [2Fe-2S] cluster binding to individual cysteine-rich motifs.
  • Temperature-dependent studies to investigate electronic transitions.
  • Involvement in electron transfer assays with the protein partner Ndor1.

Main Results:

  • Each motif independently binds a [2Fe-2S] cluster, with mutual exclusion of the second binding site.
  • Reduced [2Fe-2S](+) clusters exhibit unique electronic structures and coordination anisotropy.
  • The CX2CX7CX2C motif displays a temperature-dependent valence transition, while only the CX8CX2CXC motif participates in electron transfer with Ndor1.

Conclusions:

  • The CIAPIN1 domain's flexibility contributes to the unique electronic properties of bound [2Fe-2S] clusters.
  • Only the [2Fe-2S] cluster bound to the CX8CX2CXC motif is critical for the electron transfer chain in cytosolic Fe/S protein assembly.