NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases

J Inorg Biochem. 2017 Dec:177:384-394. doi: 10.1016/j.jinorgbio.2017.08.032. Epub 2017 Sep 4.

Abstract

The non-haem Fe(II) and 2-oxoglutarate (2OG)-dependent oxygenases belong to a superfamily of structurally-related enzymes that play important biological roles in plants, microorganisms and animals. Structural, mechanistic and functional studies of 2OG oxygenases require efficient and effective biophysical tools. Nuclear magnetic resonance (NMR) spectroscopy is a useful tool to study this enzyme superfamily. It has been applied to obtain information about enzyme kinetics, identify and characterise 2OG oxygenase-catalysed oxidation products, elucidate the catalytic mechanism, monitor ligand binding and study protein dynamics. This review summarises the types of information that NMR spectroscopy can provide in the studies of 2OG oxygenases, highlights the advantages of the technique and describes its drawbacks.

Keywords: 2OG oxygenase; DSBH/Cupin fold; Enzyme inhibition; Enzyme kinetics; Enzyme mechanism; NMR spectroscopy; Protein dynamics.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Iron / chemistry*
  • Ketoglutaric Acids / metabolism*
  • Kinetics
  • Ligands
  • Magnetic Resonance Spectroscopy / methods*
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / metabolism*
  • Models, Chemical
  • Protein Binding

Substances

  • Ketoglutaric Acids
  • Ligands
  • Iron
  • Mixed Function Oxygenases