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Bonding in Metals02:32

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Metallic bonds are formed between two metal atoms. A simplified model to describe metallic bonding has been developed by Paul Drüde called the “Electron Sea Model”. 
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Metallic solids such as crystals of copper, aluminum, and iron are formed by metal atoms. The structure of metallic crystals is often described as a uniform distribution of atomic nuclei within a “sea” of delocalized electrons. The atoms within such a metallic solid are held together by a unique force known as metallic bonding that gives rise to many useful and varied bulk properties.
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Organometallic compounds are compounds that contain a carbon–metal bond. Carbon belongs to an organyl group like alkyl, aryl, allyl, or benzyl groups. The metal can be from Group I or Group II of the periodic table, a transition metal, or a semimetal.
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Transition metals are defined as those elements that have partially filled d orbitals. As shown in Figure 1, the d-block elements in groups 3–12 are transition elements. The f-block elements, also called inner transition metals (the lanthanides and actinides), also meet this criterion because the d orbital is partially occupied before the f orbitals.
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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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As early chemists discovered more elements, they realized that various elements could be grouped by their similar chemical behaviors. One such grouping includes lithium (Li), sodium (Na), and potassium (K). All of these elements are shiny, conduct heat and electricity well, and have similar chemical properties. A second grouping includes calcium (Ca), strontium (Sr), and barium (Ba), which also are shiny, good conductors of heat and electricity, and have chemical properties in common. However,...
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Metal preferences and metallation.

Andrew W Foster1, Deenah Osman1, Nigel J Robinson2

  • 1From the Department of Chemistry and School of Biological and Biomedical Sciences, Durham University, Durham DH1 3LE, United Kingdom.

The Journal of Biological Chemistry
|August 28, 2014
PubMed
Summary

Most metalloenzymes require specific metals not matching their natural binding preferences. Cells use buffered metal pools and delivery systems to ensure correct metallation, especially for enzymes lacking dedicated cofactor assembly pathways.

Keywords:
CopperIronIrving-Williams SeriesManganeseMetal SensorsMetallochaperoneMetalloenzymesNickelPolydisperse BufferZinc

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Metalloenzymes require specific metal ions for function, but cellular metal concentrations and protein binding affinities often mismatch.
  • Approximately 30% of metalloenzymes utilize dedicated metal delivery systems or preassembled metal cofactors for efficient metallation.
  • The remaining 70% of metalloenzymes are thought to rely on competition within buffered intracellular metal pools.

Purpose of the Study:

  • To elucidate the mechanisms cells employ to ensure correct metallation of metalloenzymes.
  • To explain how cells manage metal ion availability and binding preferences to meet metalloenzyme requirements.

Main Methods:

  • The study infers cellular metallation strategies based on known metal binding preferences of metalloproteins and metal ion properties.
  • It analyzes the interplay between buffered metal concentrations and metal-ligand complex stability.

Main Results:

  • Cellular metallation is facilitated by maintaining intracellular metal pool concentrations inversely proportional to the stability of their respective metal complexes.
  • For instance, magnesium enzymes exhibit a preference for zinc, leading to zinc concentrations being maintained at least a million-fold lower than magnesium inside cells.
  • This regulatory strategy ensures that less stable metal complexes, like those involving magnesium, can effectively compete for binding sites.

Conclusions:

  • Cells actively regulate intracellular metal ion concentrations to overcome the inherent metal binding preferences of metalloenzymes.
  • Buffered metal pools, adjusted based on complex stability, are crucial for the proper metallation of the majority of metalloenzymes.
  • Understanding these mechanisms is vital for comprehending cellular metal homeostasis and enzyme function.