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PMID: 15739104 Published · ppublish English Journal Article Review

The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes.

Koehntop KD, Emerson JP, Que L

Abstract

General knowledge of dioxygen-activating mononuclear non-heme iron(II) enzymes containing a 2-His-1-carboxylate facial triad has significantly expanded in the last few years, due in large part to the extensive library of crystal structures that is now available. The common structural motif utilized by this enzyme superfamily acts as a platform upon which a wide assortment of substrate transformations are catalyzed. The facial triad binds a divalent metal ion at the active site, which leaves the opposite face of the octahedron available to coordinate a variety of exogenous ligands. The binding of substrate activates the metal center for attack by dioxygen, which is subsequently converted to a high-valent iron intermediate, a formidable oxidizing species. Herein, we summarize crystallographic and mechanistic features of this metalloenzyme superfamily, which has enabled the proposal of a common but flexible pathway for dioxygen activation.

MeSH Terms
Binding Sites Catalysis Enzymes/chemistry,metabolism Models, Chemical Models, Molecular Molecular Structure Nonheme Iron Proteins/chemistry,metabolism Oxygen/chemistry,metabolism
Chemicals
Enzymes Nonheme Iron Proteins Oxygen
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Koehntop Kevin D
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, 55455, USA.
Emerson Joseph P
Que Lawrence
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Article Info
Journal
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
Abbr.
J Biol Inorg Chem
ISSN
0949-8257
Published
2005-03-00
Epub
2005-00-01
Pages
87-93
Language
English
Region
Germany
NLM ID
9616326
Subset
IM
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