Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:alpha-ketoglutarate dioxygenase (TauD).
The Fe(II)- and alpha-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:alpha-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 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.
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
John C
JC
Price
Eric W
EW
Barr
Timothy E
TE
Glass
Carsten
C
Krebs
J Martin
JM
Bollinger
D041961:Deuterium Exchange Measurement; D004926:Escherichia coli / Q000201:enzymology; D005296:Ferrous Compounds / Q000737:chemistry / Q000378:metabolism; D006859:Hydrogen / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism*; D015204:Spectroscopy, Mossbauer / Q000379:methods; D013654:Taurine / Q000737:chemistry
D005296:Ferrous Compounds; D013654:Taurine; D006859:Hydrogen; D006899:Mixed Function Oxygenases; C433064:taurine-alpha-ketoglutarate dioxygenase; D010100:Oxygen