Journal
DALTON TRANSACTIONS
Volume -, Issue 38, Pages 5132-5142Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b803512a
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Funding
- NIH [GM063584]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM063584] Funding Source: NIH RePORTER
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Fe-II/alpha-ketoglutarate-dependent hydroxylases uniformly possess a double-stranded beta-helix fold with two conserved histidines and one carboxylate coordinating their mononuclear ferrous ions. Oxidative decomposition of the alpha-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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