The ability of green fluorescent proteins for photoconversion under oxygen-free conditions is determined by the chromophore structure rather than its amino acid environment

Yu V. Kiseleva, A. S. Mishin, A. M. Bogdanov, Yu A. Labas, K. A. Luk'yanov

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Photoconversion of various green and cyan fluorescent proteins to the red fluorescent state under the oxygen-free conditions was studied. Such photoconversion has earlier been described for the EGFP green fluorescent protein. Phylogenetically distant fluorescent proteins that have a low identity of their amino acid sequences but contain chemically identical chromophores based on a Tyr residue were shown to be susceptible to this type of photoconversion. At the same time, the ECFP protein, which has 92% homology with EGFP but contains a chromophore based on tryptophan did not undergo the photoconversion. Thus, it is precisely the chromophore structure, rather than the amino acid environment that determines the ability of green fluorescent proteins to display photoconversion to the red fluorescent state under anaerobic conditions.

Original languageEnglish
Pages (from-to)638-641
Number of pages4
JournalRussian Journal of Bioorganic Chemistry
Volume34
Issue number5
DOIs
Publication statusPublished - Sep 2008
Externally publishedYes

Keywords

  • Fluorescent labeling
  • Green fluorescent protein
  • Photoconversion

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