Taurine/a-ketoglutarate dioxygenase TauD

Price JC, Barr EW, Tirupati B, Bollinger JM Jr, Krebs C. The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase a high-spin FePV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 2003 42 7497-7508. 

Only since 2003 has there been spectroscopic evidence to support that monomeric, nonheme iron oxygenases cleave O2 and form Fe(IV)=0 species. These findings came from studies on taurine dioxygenase (TauD), a member of the Fe(If)/a-ketoglutarate (a-KG)-dependent hydroxylase superfamily of enzymes [48]. A generic mechanism proposed for hydroxylation is shown in Fig. 6.19 and includes an Fe(IV)=0 intermediate as the competent H-atom abstractor. 

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