Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Iron Proteins, Mononuclear (non-heme) Iron Oxygenases

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_357
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Synonyms

 Dioxygenase;  Mixed-function-oxidase;  Monooxygenase;  Oxygenase

Definitions

Mononuclear nonheme iron oxygenases are a large group of iron-containing enzymes known to catalyze the transfer of one or both oxygen atoms from dioxygen (O2) into organic substrates.

Introduction

Mononuclear nonheme iron oxygenases (Costas et al. 2004; Bruijnincx et al. 2008; Kovaleva and Lipscomb 2008) are distinct from the more familiar heme-dependent oxygenases primarily due to the set of ligands used to coordinate the catalytic iron atom. Ligands to the nonheme sites are protein-derived amino acids (most commonly His, Tyr, Asp, and Glu) along with solvent molecules, while heme sites utilize a porphyrin macrocyclic ring to coordinate the metal. Consequently, the nonheme iron sites exhibit a much wider diversity of metal site ligand compositions and coordination geometries (Solomon et al. 2003). One ramification of this structural diversity is that nonheme sites are known to stabilize iron at...

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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of Biochemistry, Molecular Biology, and BiophysicsUniversity of MinnesotaMinneapolisUSA