Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study.
A wide range of spectroscopic approaches have been used to interrogate the mononuclear iron metallocenter in 2-oxoglutarate (2OG)-dependent oxygenases. The results from these spectroscopic studies have provided valuable insights into the structural changes at the active site during substrate binding and catalysis, thus providing critical information that complements investigations of these enzymes by X-ray crystallography, biochemical, and computational approaches. This mini-review highlights taurine hydroxylase (taurine:2OG dioxygenase, TauD) as a case study to illustrate the wealth of knowledge that can be generated by applying a diverse array of spectroscopic investigations to a single enzyme. In particular, electronic absorption, circular dichroism, magnetic circular dichroism, conventional and pulse electron paramagnetic, Mössbauer, X-ray absorption, and resonance Raman methods have been exploited to uncover the properties of the metal site in TauD.
Department of Chemistry, Michigan State University, East Lansing, MI, 48824, USA.
Denis A
DA
Proshlyakov
Department of Chemistry, Michigan State University, East Lansing, MI, 48824, USA.
John
J
McCracken
Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI, 48824, USA. hausinge@msu.edu.|Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, 48824, USA. hausinge@msu.edu.
Robert P
RP
Hausinger
D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis / Q000379:methods*
D006899:Mixed Function Oxygenases; C433064:taurine-alpha-ketoglutarate dioxygenase
2-Oxoglutarate; Nonheme iron; Oxygenase; Spectroscopy