Spectral tuning of photoactive yellow protein

T. Yamato, T. Ishikura, T. Kakitani, K. Kawaguchi, H. Watanabe

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


We report a theoretical study on the optical properties of a small, water-soluble photosensory receptor, photoactive yellow protein (PYP). A hierarchical ab initio molecular orbital calculation accurately evaluated the optical absorption maximum of the wild-type, as well as the λ max values of 12 mutants. Electronic excitation of the chromophore directly affects the electronic state of nearby atoms in the protein environment. This effect is explicitly considered in the present study. Furthermore, the spectral tuning mechanism of PYP was investigated at the atomic level. The static disorder of a protein molecule is intimately related to the complex nature of its energy landscape. By using molecular dynamics simulation and quantum mechanical structure optimization, we obtained multiple minimum energy conformations of PYP. The statistical distribution of electronic excitation energies of these minima was compared with the hole-burning experiment (Masciangioli, T. [2000]Photochem. Photobiol. 72, 639), a direct observation of the distribution of excitation energies.

Original languageEnglish
Pages (from-to)323-327
Number of pages5
JournalPhotochemistry and Photobiology
Issue number2
Publication statusPublished - 2007 Mar 1
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry


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