Stabilization of structure in near-infrared fluorescent proteins by binding of biliverdin chromophore

Olesya V. Stepanenko, Olga V. Stepanenko, G. S. Bublikov, I. M. Kuznetsova, Vladislav Verkhusha, K. K. Turoverov

Research output: Contribution to journalArticle

8 Scopus citations


Near-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochromes and their mutants with different location of Cys residues, which able to bind a biliverdin chromophore, or without these Cys residues were studied using intrinsic tryptophan fluorescence, NIR fluorescence and circular dichroism. It was shown that a covalent binding of the biliverdin chromophore to a Cys residue via thioether group substantially stabilizes the spatial structure of NIR FPs. The stability of the protein structure and the chromophore association strength strongly depends on the location of Cys residues and decreases in the following order: a protein with Cys residues in both domains, a protein with Cys in PAS domains, and a protein with Cys in GAF domains. NIR FPs without Cys residues capable to covalently attach biliverdin have the lowest stability, comparable to NIR FP apoforms.

Original languageEnglish (US)
JournalJournal of Molecular Structure
StateAccepted/In press - Aug 2 2016


  • Bacterial phytochrome
  • Biliverdin
  • BphP1-FP
  • IRFP
  • Near-infrared fluorescent probe
  • Stability

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy
  • Organic Chemistry
  • Inorganic Chemistry

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