Abstract
The 2-oxoglutarate (2OG)-dependent oxygenases utilize dioxygen and 2OG to oxidize a wide variety of substrates. Over the past two decades, a number of Fe(ii)-containing model systems of structural relevance to 2OG-dependent enzymes utilizing tripodal ligand frameworks and 2-oxo acids have provided great insight into the reactivity of these enzymes. Like the 2OG-dependent enzymes, the model complexes react with dioxygen and carry out the oxidative decarboxylation of a 2-oxoacid to generate a potent oxidant that is likely to be an Fe(iv)O intermediate. Over the past 12 years, many Fe(iv)O complexes have been synthesized, spanning a variety of ligand motifs, coordination geometries and spin states. This chapter reviews the synthetic strategies applied to generating both functional models of the reactions carried out by 2OG-dependent enzymes, as well as spectroscopic models of relevance to transient reaction intermediates. A focus is given to advances in understanding of the enzymatic reaction obtained from studying the reactivity of these synthetic systems.
Original language | English (US) |
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Title of host publication | 2-Oxoglutarate-Dependent Oxygenases |
Editors | Robert P. Hausinger, Christopher J. Schofield |
Publisher | Royal Society of Chemistry |
Pages | 123-148 |
Number of pages | 26 |
Edition | 3 |
DOIs | |
State | Published - 2015 |
Publication series
Name | RSC Metallobiology |
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Number | 3 |
Volume | 2015-January |
ISSN (Print) | 2045-547X |
Bibliographical note
Publisher Copyright:© 2015 The Royal Society of Chemistry.