Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study

  • Denis A. Proshlyakov
  • John McCracken
  • Robert P. Hausinger
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Part of the following topical collections:
  1. 60 Years of Oxygen Activation

Abstract

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.

Keywords

2-Oxoglutarate Nonheme iron Oxygenase Spectroscopy 

Abbreviations

CD

Circular dichroism

CF

Continuous flow

cw

Continuous wave

DOPA

Dihydroxyphenylalanine

EPR

Electron paramagnetic resonance

ESEEM

Electron spin echo envelope modulation

EXAFS

Extended X-ray absorption fine structure

FQ

Freeze quench

FT

Fourier transform

HYSCORE

Hyperfine sublevel correlation

LMCT

Ligand-to-metal charge-transfer

MCD

Magnetic circular dichroism

MLCT

Metal-to-ligand charge-transfer

2OG

2-Oxoglutarate

RR

Resonance Raman

SF

Stopped-flow

TauD

Taurine:2OG dioxygenase

UV

Ultraviolet

XAS

X-ray absorption spectroscopy

Notes

Acknowledgements

Work in the authors’ laboratories on this topic was supported by the National Institutes of Health (GM096132 to DAP, GM054065 and RR15880 to JM, and GM063584 to RPH).

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Copyright information

© SBIC 2016

Authors and Affiliations

  • Denis A. Proshlyakov
    • 1
  • John McCracken
    • 1
  • Robert P. Hausinger
    • 2
    • 3
  1. 1.Department of ChemistryMichigan State UniversityEast LansingUSA
  2. 2.Department of Microbiology and Molecular GeneticsMichigan State UniversityEast LansingUSA
  3. 3.Department of Biochemistry and Molecular BiologyMichigan State UniversityEast LansingUSA

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