1.14.11.17	657933	X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates	Biochemistry	41	5185-5192	2002	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/11955067/	
1.14.11.17	743152	Atom tunneling in the hydroxylation process of taurine/alpha-ketoglutarate dioxygenase identified by quantum mechanics/molecular mechanics simulations	J. Phys. Chem. B	121	5347-5354	2017	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/28490178/	
1.14.11.17	657996	Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure	Biochemistry	42	5547-5554	2003	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/12741810/	
1.14.11.17	685159	Probing the iron-substrate orientation for taurine/alpha-ketoglutarate dioxygenase using deuterium electron spin echo envelope modulation spectroscopy	Biochemistry	46	5951-5959	2007	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/17469855/	
1.14.11.17	701264	Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine a ketoglutarate dioxygenase (TauD)	Tetrahedron Lett.	50	611-613	2009	Escherichia coli	-	
1.14.11.17	687288	Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant	J. Am. Chem. Soc.	129	6168-6179	2007	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/17451240/	
1.14.11.17	674930	Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism	J. Biol. Inorg. Chem.	11	63-72	2006	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/16320009/	
1.14.11.17	671301	An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation	Anal. Biochem.	353	69-74	2006	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/16643838/	
1.14.11.17	697475	Elucidating enzyme mechanism and intrinsic chemical properties of short-lived intermediates in the catalytic cycles of cysteine dioxygenase and taurine/alpha-ketoglutarate dioxygenase	Coord. Chem. Rev.	253	754-768	2009	Homo sapiens	-	
1.14.11.17	765270	Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD	J. Phys. Chem. B	123	7785-7793	2019	Escherichia coli	https://pubmed.ncbi.nlm.nih.gov/31433947/