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Structural Isomerism02:34

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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.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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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.
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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...
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CFT focuses on...
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Color in Coordination Complexes
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Structure/function correlations over binuclear non-heme iron active sites.

Edward I Solomon1, Kiyoung Park2

  • 1Department of Chemistry, Stanford University, Stanford, CA, 94305-5080, USA. edward.solomon@stanford.edu.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|July 3, 2016
PubMed
Summary
This summary is machine-generated.

Binuclear non-heme iron enzymes use three distinct mechanisms to bind and activate O2. Variable-temperature, variable-field magnetic circular dichroism spectroscopy (VTVH MCD) revealed these pathways for diverse iron enzyme active sites.

Keywords:
Binuclear non-heme iron enzymesFrontier molecular orbitalsO2 activationPeroxide activationVariable-temperature, variable-field magnetic circular dichroism

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Spectroscopy

Background:

  • Binuclear non-heme iron enzymes are crucial for biological O2 activation.
  • Understanding O2 binding mechanisms is key to enzyme function.

Purpose of the Study:

  • To elucidate the structural mechanisms of O2 binding to coupled binuclear iron sites.
  • To differentiate O2 activation pathways in various enzyme active sites.

Main Methods:

  • Variable-temperature, variable-field magnetic circular dichroism (VTVH MCD) spectroscopy.
  • Analysis of different binuclear iron active site structures (μ-OH-bridged, carboxylate-bridged).

Main Results:

  • Identified three distinct O2 binding mechanisms: terminal hydroperoxide, bridged peroxide, and one-electron O2- or NO- adducts.
  • Hemerythrin utilizes a proton-coupled electron transfer mechanism for O2 binding.
  • Carboxylate-bridged sites show varied O2 binding depending on coordination unsaturation.

Conclusions:

  • O2 activation by binuclear non-heme iron enzymes is mechanistically diverse.
  • VTVH MCD is a powerful tool for characterizing these complex iron sites.
  • Further strategies for peroxo-intermediate activation are proposed.