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Metallocenter Biosynthesis & Assembly

  1. Scott B. Mulrooney,
  2. Robert P. Hausinger

Published Online: 15 MAR 2013

DOI: 10.1002/9781119951438.eibc0257.pub2

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Mulrooney, S. B. and Hausinger, R. P. 2013. Metallocenter Biosynthesis & Assembly . Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. Michigan State University, East Lansing, MI, USA

Publication History

  1. Published Online: 15 MAR 2013


Cells synthesize biological metallocenters by use of several recurring themes, often with multiple themes combined into a single pathway. In the simplest situation, binding of a metal ion to a biological ligand occurs by reversible thermodynamic control; however, the prevalence of metallocenters deeply buried within macromolecules, the exceedingly low concentrations of free metal ions within cells, and the sophisticated structures of many metal-containing active sites and cofactors provide evidence that alternative and more complex approaches must also exist. In some cases, metal binding is accompanied by posttranslational modification of the target protein, either before or after the metal binds. Many metallocenters contain additional components that are added along with the metal ion. In other cases, metallochaperones are used to deliver the metal of interest to an apoprotein. Another alternative is to incorporate the metal into a protein subunit that subsequently swaps for an apoprotein subunit in the native protein. In addition, electron-transfer reactions may be coupled with metal assembly. Other proteins require a preassembled metal-containing cofactor rather than just the free metal ions. The cofactor may bind reversibly or be delivered by a chaperone, and scaffolding proteins may be used to provide a framework for construction of such a cofactor. Covalent attachment of the cofactor occurs in some cases. Finally, molecular chaperones that directly or indirectly alter the conformation of the target apoprotein may be utilized. In many cases, the function of the molecular chaperone is coupled to nucleotide triphosphate hydrolysis. Examples are provided for each of these metallocenter biosynthetic mechanisms.


  • apoprotein;
  • cofactor;
  • heme;
  • iron-sulfur clusters;
  • metallochaperone;
  • metallocenter;
  • molybdopterin;
  • scaffold proteins