Chromophore formation in DsRed occurs by a branched pathway

J Am Chem Soc. 2010 Jun 23;132(24):8496-505. doi: 10.1021/ja1030084.

Abstract

Like GFP, the fluorescent protein DsRed has a chromophore that forms autocatalytically within the folded protein, but the mechanism of DsRed chromophore formation has been unclear. It was proposed that an initial oxidation generates a green chromophore, and that a final oxidation yields the red chromophore. However, this model does not adequately explain why a mature DsRed sample contains a mixture of green and red chromophores. We present evidence that the maturation pathway for DsRed branches upstream of chromophore formation. After an initial oxidation step, a final oxidation to form the acylimine of the red chromophore is in kinetic competition with a dehydration to form the green chromophore. This scheme explains why green and red chromophores are alternative end points of the maturation pathway.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Color
  • Hydrogen Peroxide / chemistry
  • Kinetics
  • Luminescent Proteins / chemistry*
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Models, Chemical
  • Mutation
  • Oxidation-Reduction
  • Oxygen / chemistry
  • Solubility

Substances

  • Luminescent Proteins
  • fluorescent protein 583
  • Hydrogen Peroxide
  • Oxygen