Standard Article

Iron Proteins with Mononuclear Active Sites

  1. Joseph P. Emerson,
  2. Mark P. Mehn,
  3. Lawrence Que Jr

Published Online: 15 DEC 2011

DOI: 10.1002/9781119951438.eibc0106

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Emerson, J. P., Mehn, M. P. and Que, L. 2011. Iron Proteins with Mononuclear Active Sites. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. University of Minnesota, Minneapolis, MN, USA

Publication History

  1. Published Online: 15 DEC 2011

Abstract

Metalloenzymes containing a mononuclear nonheme iron center are often involved in dioxygen metabolism. We have divided this superfamily of enzymes into seven subcategories: iron superoxide dismutase and superoxide reductase, lipoxygenase, catechol dioxygenases, α-keto acid-dependent enzymes, isopenicillin N synthase, pterin-dependent hydroxylases, and Rieske dioxygenases. The degree of catalytic versatility and coordination flexibility encompassed by these enzymes is unsurpassed by any other known metalloenzyme superfamily. Herein we discuss the present state of knowledge regarding their active site structures and the critical role the metal center plays in their respective catalytic mechanisms.

Keywords:

  • dioxygen;
  • superoxide;
  • lipoxygenase;
  • dioxygenase;
  • monooxygenase;
  • extradiol;
  • intradiol;
  • pterin;
  • Rieske;
  • 2-oxoglutarate;
  • model complexes