Mechanism of taurine: α-ketoglutarate dioxygenase (TauD) from Escherichia coli

Joseph M. Bollinger, Jr., John C. Price, Lee M. Hoffart, Eric W. Barr, Carsten Krebs

Research output: Contribution to journalShort survey

134 Scopus citations

Abstract

The iron(II)- and α-ketoglutarate-dependent dioxygenases comprise enzymes that catalyze a variety of important reactions in biology, including steps in the biosynthesis of collagen and antibiotics, the degradation of xenobiotics, the repair of alkylated DNA, and the sensing of oxygen and response to hypoxia. In these reactions, the reductive activation of oxygen is coupled to hydroxylation of the substrate and decarboxylation of the co-substrate, α-ketoglutarate. It is believed that a single, conserved mechanistic pathway for formation of a high-valent iron intermediate that attacks the substrate is operant in all members of this family. Application of a combination of rapid kinetic and spectroscopic techniques to the reaction of taurine/α-ketoglutarate dioxygenase (TauD), one member of this large enzyme family, has led to the detection of two reaction intermediates. The first intermediate, which is termed J, is a high-spin FeIV-oxo complex. Decay of J exhibits a large, normal C1 deuterium kinetic isotope effect, demonstrating that it is the species activating the C-H bond for hydroxylation. The second intermediate is an FeII-containing product(s) complex.

Original languageEnglish (US)
Pages (from-to)4245-4254
Number of pages10
JournalEuropean Journal of Inorganic Chemistry
Issue number21
DOIs
StatePublished - Nov 4 2005

All Science Journal Classification (ASJC) codes

  • Inorganic Chemistry

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