Evidence for Hydrogen Abstraction from C1 of Taurine by the High-Spin Fe(IV) Intermediate Detected during Oxygen Activation by Taurine:α-Ketoglutarate Dioxygenase (TauD)
Top Cited Papers
- 1 October 2003
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 125 (43) , 13008-13009
- https://doi.org/10.1021/ja037400h
Abstract
The Fe(II)- and α-ketoglutarate-dependent dioxygenases catalyze hydroxylation reactions of considerable biomedical and environmental significance. Recently, the first oxidized iron intermediate in the reaction of a member of this family, taurine:α-ketoglutarate dioxygenase (TauD), was detected and shown to be a high-spin, formally Fe(IV) complex. The demonstration in this study that decay of the Fe(IV) complex is ∼30-fold slower when it is formed in the presence of 1-[2H]2-taurine provides evidence that the intermediate abstracts hydrogen from C1, the site of hydroxylation, and suggests that quantum-mechanical tunneling may contribute to C1−H cleavage.Keywords
This publication has 2 references indexed in Scilit:
- The First Direct Characterization of a High-Valent Iron Intermediate in the Reaction of an α-Ketoglutarate-Dependent Dioxygenase: A High-Spin Fe(IV) Complex in Taurine/α-Ketoglutarate Dioxygenase (TauD) from Escherichia coliBiochemistry, 2003
- Geometric and Electronic Structure/Function Correlations in Non-Heme Iron EnzymesChemical Reviews, 1999