Spectral tuning of obelin bioluminescence by mutations of Trp92

FEBS Lett. 2003 Nov 6;554(1-2):184-8. doi: 10.1016/s0014-5793(03)01166-9.

Abstract

The Ca(2+)-regulated photoprotein obelin was substituted at Trp92 by His, Lys, Glu, and Arg. All mutants fold into stable conformations and produce bimodal bioluminescence spectra with enhanced contribution from a violet emission. The W92R mutant has an almost monomodal bioluminescence (lambdamax=390 nm) and monomodal fluorescence (lambdamax=425 nm) of the product. Results are interpreted by an excited state proton transfer mechanism involving the substituent side group and His22 in the binding cavity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Calcium / analysis
  • Fluorescence
  • Luminescence*
  • Luminescent Proteins / chemistry*
  • Luminescent Proteins / genetics
  • Molecular Probes
  • Mutagenesis, Site-Directed
  • Spectrum Analysis
  • Tryptophan*

Substances

  • Luminescent Proteins
  • Molecular Probes
  • obelin
  • Tryptophan
  • Calcium