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Coordination Number and Geometry02:57

Coordination Number and Geometry

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For transition metal complexes, the coordination number determines the geometry around the central metal ion. Table 1 compares coordination numbers to molecular geometry. The most common structures of the complexes in coordination compounds are octahedral, tetrahedral, and square planar.
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In most main group element compounds, the valence electrons of the isolated atoms combine to form chemical bonds that satisfy the octet rule. For instance, the four valence electrons of carbon overlap with electrons from four hydrogen atoms to form CH4. The one valence electron leaves sodium and adds to the seven valence electrons of chlorine to form the ionic formula unit NaCl (Figure 1a). Transition metals do not normally bond in this fashion. They primarily form coordinate covalent bonds, a...
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The structure of a crystalline solid, whether a metal or not, is best described by considering its simplest repeating unit, which is referred to as its unit cell. The unit cell consists of lattice points that represent the locations of atoms or ions. The entire structure then consists of this unit cell repeating in three dimensions. The three different types of unit cells present in the cubic lattice are illustrated in Figure 1.
Types of Unit Cells
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Non-Canonical Wnt Signaling Pathways01:41

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Wnt is a zygotic effect gene that is expressed during very early embryonic development. It regulates various processes in animals starting from early development through the adult stage, such as organogenesis in the embryo and maintenance of neuronal and blood stem cells. Wnt proteins can induce a wide variety of intracellular pathways depending upon the specific abilities of different Wnt ligands to form a complex with shared and cognate receptors in the presence of different co-receptors. The...
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The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which...
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Equations of Motion: Rectangular Coordinates and Cylindrical Coordinates01:21

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Understanding the motion of particles is a fundamental aspect of classical mechanics, and the choice of the coordinate system plays a pivotal role in unraveling the complexities of their dynamics.
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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
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Engineered Metalloenzymes with Non-Canonical Coordination Environments.

Takahiro Hayashi1, Donald Hilvert1, Anthony P Green2

  • 1Laboratory of Organic Chemistry, ETH Zurich, 8093, Zurich, Switzerland.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|May 23, 2018
PubMed
Summary

Chemically programming proteins with non-canonical ligands creates novel metalloenzymes. This approach enhances understanding of bioinorganic mechanisms and enables the development of powerful new catalysts for synthetic chemistry.

Keywords:
biocatalysisdirected evolutionheme enzymesmetalloenzymesnon-canonical amino acids

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Area of Science:

  • Bioinorganic Chemistry
  • Protein Engineering
  • Catalysis

Background:

  • Nature utilizes a restricted set of amino acids for metalloenzyme active sites.
  • Cellular translation machinery can be engineered to incorporate non-canonical ligands into proteins.
  • This allows for precise tuning of metal-binding environments.

Purpose of the Study:

  • To review recent advances in creating engineered metalloenzymes with non-canonical ligands.
  • To highlight how these systems deepen the understanding of natural metalloenzyme mechanisms.
  • To explore the potential for creating novel metalloprotein catalysts with enhanced functions.

Main Methods:

  • Engineering cellular translation machinery to incorporate user-defined ligands.
  • Characterization of the resulting engineered metalloenzymes.
  • Adaptation of laboratory evolution protocols for optimization.

Main Results:

  • Demonstration of creating metalloenzymes with tailored electronic and structural properties.
  • Advancement in understanding natural bioinorganic mechanisms through studying engineered systems.
  • Successful adaptation of laboratory evolution for optimizing non-canonical ligand-containing metalloenzymes.

Conclusions:

  • Engineered metalloenzymes offer powerful chemical probes for mechanistic studies.
  • This approach merges advantages of small molecule and protein catalysis.
  • Significant promise exists for developing novel metalloprotein catalysts for valuable synthetic transformations.