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Metal-Mediated Protein Modification

  1. James W. Whittaker

Published Online: 15 MAR 2006

DOI: 10.1002/0470862106.ia274

Encyclopedia of Inorganic Chemistry

Encyclopedia of Inorganic Chemistry

How to Cite

Whittaker, J. W. 2006. Metal-Mediated Protein Modification. Encyclopedia of Inorganic Chemistry. .

Author Information

  1. Oregon Health and Science University, Beaverton, OR, USA

Publication History

  1. Published Online: 15 MAR 2006

Abstract

Posttranslational modification of proteins is a general mechanism for regulating biological activity and expanding the functionality in this family of biopolymers. Metal ions have been found to be intimately involved in many of these protein-processing reactions, whether as cofactors of processing metalloenzymes, intrinsic cofactors for self-processing proteins, or protein-targeting solution complexes. A broad range of covalent modifications have been identified as the products of these metal-mediated reactions. Novel amino acid residues resulting from oxygenation, oxidation, or cross-linking side chains play important roles in the structure and reactivity of proteins. In a number of cases, the modified amino acids serve as built-in catalytic cofactors. Reactions of certain metal complexes have been implicated in biomedically important protein modifications, and synthetic complexes have been developed as probes of macromolecular structure. These links underscore the close connections between inorganic and biological chemistry.

Keywords:

  • metalloprotein;
  • metalloenzyme;
  • posttranslational modification;
  • self-processing;
  • biogenesis;
  • quinoenzyme;
  • quinocofactor