@inbook{c0964eea269f47bd92f84dad566e3ad5,
title = "Synthetic models of 2-oxoglutarate-dependent oxygenases",
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.",
author = "Allpress, {Caleb J.} and Kleespies, {Scott T.} and Lawrence Que",
year = "2015",
month = jan,
day = "1",
doi = "10.1039/9781782621959-00123",
language = "English (US)",
series = "RSC Metallobiology",
publisher = "Royal Society of Chemistry",
number = "3",
pages = "123--148",
editor = "Hausinger, {Robert P.} and Schofield, {Christopher J.}",
booktitle = "2-Oxoglutarate-Dependent Oxygenases",
edition = "3",
}