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PMID: 9461283 Published · ppublish English Journal Article Review

The 2-His-1-carboxylate facial triad--an emerging structural motif in mononuclear non-heme iron(II) enzymes.

European journal of biochemistry ·Vol. 250 ·No. 3 ·1997-12-15 ·Pages 625-9

Hegg EL, Que L

Abstract

A 2-His-1-carboxylate facial triad is a common feature of the active sites in a number of mononuclear non-heme iron(II) enzymes. This structural motif was established crystallographically for five different classes of enzymes and inferred from sequence similarity for two other classes. The 2-His-1-carboxylate facial triad anchors the iron in the active site and at the same time maintains three additional cis-oriented sites. These sites can be used to bind other endogenous ligands or exogenous ligands such as substrate and/or O2, giving the metal center great flexibility to use different mechanistic strategies to perform a variety of chemical transformations.

MeSH Terms
Binding Sites Catalysis Crystallography, X-Ray Enzymes/chemistry,metabolism Iron/chemistry Ligands Nonheme Iron Proteins/chemistry Oxygen/metabolism
Chemicals
Enzymes Ligands Nonheme Iron Proteins Iron Oxygen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hegg E L
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis 55455, USA.
Que L
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1997-12-15
Pages
625-9
Language
English
Region
England
NLM ID
0107600
Subset
IM
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