John C. Price

TL;DR: An oxidized Fe intermediate in the reaction of one of these enzymes, taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli, has been directly demonstrated by rapid kinetic and spectroscopic methods, suggesting that the iron ligands in the TauD intermediate confer significant Fe(III) character to the high-valent site by strong electron donation.

TL;DR: The developed methodology can be adapted to assess in vivo proteome homeostasis in any model organism that will tolerate a labeled diet and may be particularly useful in the analysis of neurodegenerative diseases in vivo.

TL;DR: The demonstration in this study that decay of the Fe(IV) complex is approximately 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.

TL;DR: X-ray absorption spectroscopy is used to demonstrate the presence of a short (1.62 A) interaction between the iron and one of its ligands in the Fe(IV) intermediate but not in theFe(II) starting complex, which strongly corroborates the hypothesis that the intermediate contains an Fe=O structural motif.

TL;DR: 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.