Synthetic models of 2-oxoglutarate-dependent oxygenases

Caleb J. Allpress, Scott T. Kleespies, Lawrence Que

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

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 languageEnglish (US)
Title of host publication2-Oxoglutarate-Dependent Oxygenases
EditorsRobert P. Hausinger, Christopher J. Schofield
PublisherRoyal Society of Chemistry
Pages123-148
Number of pages26
Edition3
DOIs
StatePublished - 2015

Publication series

NameRSC Metallobiology
Number3
Volume2015-January
ISSN (Print)2045-547X

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