Evidence for redox forms of the Aequorea green fluorescent protein

FEBS Lett. 1994 Sep 5;351(2):211-4. doi: 10.1016/0014-5793(94)00859-0.

Abstract

Highly purified recombinant Aequorea green fluorescent protein is able to undergo a reversible oxidation-reduction reaction in the presence of molecular oxygen. In the oxidized form in near UV light, the protein is highly fluorescent, but when reduced with sodium dithionite, it becomes completely non-fluorescent. On exposure to molecular oxygen the reduced, non-fluorescent protein reverts to its original fluorescent state.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Fluorescence
  • Green Fluorescent Proteins
  • Luminescent Proteins / chemistry*
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Oxygen / metabolism
  • Recombinant Fusion Proteins / chemistry
  • Scyphozoa / chemistry*
  • Scyphozoa / metabolism
  • Spectrometry, Fluorescence
  • Spectrophotometry

Substances

  • Luminescent Proteins
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Oxygen

Associated data

  • GENBANK/L29345