Fluorescent proteins: maturation, photochemistry and photophysics

Curr Opin Struct Biol. 2006 Dec;16(6):714-21. doi: 10.1016/j.sbi.2006.10.001. Epub 2006 Oct 24.


It has long been appreciated that green fluorescent protein (GFP) autocatalytically forms its chromophore in a host-independent process; several of the initial steps in the reaction have recently been elucidated. Nevertheless, the end points of the process are unexpectedly diverse, as six chemically distinct chromophores, including two with three rings, have been identified. All fluorescent proteins continuously produce a low level of reactive oxygen species under illumination, which, in some cases, can lead to host cell death. In one extreme but useful example, the red fluorescent protein KillerRed can be used to selectively destroy cells upon brief illumination. Finally, when photophysical processes such as excited-state proton transfer, reversible photobleaching and photoactivation are understood, useful research tools, for example, real-time biosensors and optical highlighters, can result; however, side effects of their use may lead to significant artifacts in time-dependent microscopy experiments.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Chemical Phenomena
  • Chemistry, Physical
  • Green Fluorescent Proteins / chemistry
  • Green Fluorescent Proteins / metabolism
  • In Vitro Techniques
  • Luminescent Proteins / chemistry*
  • Luminescent Proteins / metabolism*
  • Models, Molecular
  • Photochemistry
  • Protein Folding
  • Protons


  • Luminescent Proteins
  • Protons
  • Green Fluorescent Proteins