Metal preferences and metallation

J Biol Chem. 2014 Oct 10;289(41):28095-103. doi: 10.1074/jbc.R114.588145. Epub 2014 Aug 26.

Abstract

The metal binding preferences of most metalloproteins do not match their metal requirements. Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with ∼ 25% acquiring preassembled metal cofactors. The remaining ∼ 70% are presumed to compete for metals from buffered metal pools. Metallation is further aided by maintaining the relative concentrations of these pools as an inverse function of the stabilities of the respective metal complexes. For example, magnesium enzymes always prefer to bind zinc, and these metals dominate the metalloenzymes without metal delivery systems. Therefore, the buffered concentration of zinc is held at least a million-fold below magnesium inside most cells.

Keywords: Copper; Iron; Irving-Williams Series; Manganese; Metal Sensors; Metallochaperone; Metalloenzymes; Nickel; Polydisperse Buffer; Zinc.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacillus subtilis / chemistry
  • Bacillus subtilis / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Biological Transport
  • Clostridium / chemistry
  • Clostridium / metabolism
  • Cyanobacteria / chemistry
  • Cyanobacteria / metabolism
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism
  • Helicobacter pylori / chemistry
  • Helicobacter pylori / metabolism
  • Iron / chemistry*
  • Iron / metabolism
  • Kinetics
  • Magnesium / chemistry
  • Magnesium / metabolism
  • Manganese / chemistry*
  • Manganese / metabolism
  • Metalloproteins / chemistry*
  • Metalloproteins / metabolism
  • Models, Molecular
  • Thermodynamics
  • Zinc / chemistry*
  • Zinc / metabolism

Substances

  • Bacterial Proteins
  • Metalloproteins
  • Manganese
  • Iron
  • Magnesium
  • Zinc

Associated data

  • PDB/2VQA
  • PDB/2XL7