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Keywords:

  • Active sites;
  • Metalloproteins;
  • Proteins;
  • Metalloproteins;
  • Bioinorganic chemistry

Abstract

Manganese is an essential trace element, forming the active sites of a number of metalloproteins. Several metalloproteins contain two or more manganese ions per subunit. The structural properties of these enzymes and the experimental evidence for their proposed structures are described. Parallel to the efforts of biochemists, who are seeking to understand the function of these enzymes on a molecular level, inorganic chemists have been investigating the coordination chemistry of bi- and polynuclear complexes of manganese which contain O, N donor atoms and a variety of bridging O, N ligands. A large number of such complexes have been synthesized, their X-ray structures determined and their magnetic and spectroscopic properties studied in detail. In some instances the electronic and spectroscopic properties of these model compounds are amazingly similar to those of the biomolecules. This has led to a deeper understanding of the structure and sometimes of the function of the metalloproteins. Research on manganese metalloproteins with polynuclear active sites represents a fascinating example of interdisciplinary cooperation between physicists, biochemists and inorganic chemists.