The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase

Chem Commun (Camb). 2002 Oct 21:(20):2386-7. doi: 10.1039/b207027h.

Abstract

The inactive, nitrosyl bound form of Fe-type nitrile hydratase (NHase) contains two active site cysteine residues that are post-translationally modified to sulfenate (SO-) and sulfinate (SO2-) ligands. DFT and INDO/S calculations support the hypothesis that these unusual modifications play a key role in modulating the electronic absorption spectra and photoreactivity of the Fe(III) centre in the enzyme.

Publication types

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

MeSH terms

  • Binding Sites
  • Cysteine / metabolism
  • Hydro-Lyases / chemistry
  • Hydro-Lyases / metabolism
  • Hydro-Lyases / radiation effects*
  • Light
  • Models, Molecular
  • Nonheme Iron Proteins / chemistry
  • Nonheme Iron Proteins / metabolism
  • Nonheme Iron Proteins / radiation effects
  • Protein Processing, Post-Translational / physiology*
  • Sulfenic Acids
  • Sulfinic Acids

Substances

  • Nonheme Iron Proteins
  • Sulfenic Acids
  • Sulfinic Acids
  • Hydro-Lyases
  • nitrile hydratase
  • Cysteine