¹H-HYSCORE Reveals Structural Details at the Fe(II) Active Site of Taurine:2-Oxoglutarate Dioxygenase.

ABSTRACT: Proton Hyperfine Sublevel Correlation (¹H-HYSCORE) experiments have been used to probe the ligation structure of the Fe(II) active site of taurine:2-oxoglutarate dioxygenase (TauD), a non-heme Fe(II) hydroxylase. To facilitate Electron Paramagnetic Resonance (EPR) experiments, Fe(II) derivatives of the enzyme were studied using nitric oxide as a substitute for molecular oxygen. The addition of NO to the enzyme yields an S = 3/2 {FeNO}⁷ paramagnetic center characterized by nearly axial EPR spectra with g_⊥ = 4 and g_|| = 2. Using results from (i) an X-ray crystallographic study of TauD crystallized under anaerobic conditions in the presence of both cosubstrate 2-oxoglutarate and substrate taurine, (ii) a published theoretical description of the {FeN

SUBMITTER: McCracken J 

PROVIDER: S-EPMC8896577 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature