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

128 Citations (Scopus)

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

Fingerprint

Dioxygenases
Taurine
Escherichia coli
Hydroxylation
Substrates
Iron
Oxygen
Reaction intermediates
Kinetics
Deuterium
Biosynthesis
Xenobiotics
Enzymes
Isotopes
Repair
Collagen
Chemical activation
Anti-Bacterial Agents
Degradation
DNA

All Science Journal Classification (ASJC) codes

  • Inorganic Chemistry

Cite this

@article{b34f3290812943bcb2d3f66e73fe2f19,
title = "Mechanism of taurine: α-ketoglutarate dioxygenase (TauD) from Escherichia coli",
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.",
author = "{Bollinger, Jr.}, {Joseph M.} and Price, {John C.} and Hoffart, {Lee M.} and Barr, {Eric W.} and Carsten Krebs",
year = "2005",
month = "11",
day = "4",
doi = "10.1002/ejic.200500476",
language = "English (US)",
pages = "4245--4254",
journal = "Chemische Berichte",
issn = "0009-2940",
publisher = "Wiley-VCH Verlag",
number = "21",

}

Mechanism of taurine : α-ketoglutarate dioxygenase (TauD) from Escherichia coli. / Bollinger, Jr., Joseph M.; Price, John C.; Hoffart, Lee M.; Barr, Eric W.; Krebs, Carsten.

In: European Journal of Inorganic Chemistry, No. 21, 04.11.2005, p. 4245-4254.

Research output: Contribution to journalShort survey

TY - JOUR

T1 - Mechanism of taurine

T2 - α-ketoglutarate dioxygenase (TauD) from Escherichia coli

AU - Bollinger, Jr., Joseph M.

AU - Price, John C.

AU - Hoffart, Lee M.

AU - Barr, Eric W.

AU - Krebs, Carsten

PY - 2005/11/4

Y1 - 2005/11/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=27744579584&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=27744579584&partnerID=8YFLogxK

U2 - 10.1002/ejic.200500476

DO - 10.1002/ejic.200500476

M3 - Short survey

AN - SCOPUS:27744579584

SP - 4245

EP - 4254

JO - Chemische Berichte

JF - Chemische Berichte

SN - 0009-2940

IS - 21

ER -