FeII/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism

Jana M. Simmons; Tina A. Müller; Robert P. Hausinger

doi:10.1039/B803512A

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Dalton Transactions

Issue 38, 2008

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Fe^II/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism

Jana M. Simmons , Tina A. Müller and Robert P. Hausinger

Dalton Trans., 2008, 5132-5142

DOI: 10.1039/B803512A
Received 29 Feb 2008, Accepted 08 May 2008
First published on the web 27 Jun 2008

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Abstract
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Fe^II/α-ketoglutarate-dependent hydroxylases uniformly possess a double-stranded β-helix fold with two conserved histidines and one carboxylate coordinating their mononuclear ferrous ions. Oxidative decomposition of the α-keto acid is proposed to generate a ferryl–oxo intermediate capable of hydroxylating unactivated carbon atoms in a myriad of substrates. This Perspective focuses on a subgroup of these enzymes that are involved in pyrimidine salvage, purine decomposition, nucleoside and nucleotide hydroxylation, DNA/RNA repair, and chromatin modification. The varied reaction schemes are presented, and selected structural and kinetic information is summarized.

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Dalton Transactions

Fe^II/α-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism

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