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Absorption Spectra of Photoactive Yellow Protein Chromophores in Vacuum

I. B. Nielsen ^*, S. Boyé-Péronne , M. O. A. El Ghazaly ^*, M. B. Kristensen ^*, S. Brøndsted Nielsen ^* and L. H. Andersen ^*

^* Department of Physics and Astronomy, University of Aarhus, Aarhus, Denmark; and Laboratoire de Photophysique Moléculaire, Paris-Sud University, Orsay Cédex, France

Correspondence: Address reprint requests to L. H. Andersen, Dept. of Physics and Astronomy, University of Aarhus, DK-8000 Aarhus C, Denmark. Tel.: +45 89423605; Fax: +45 86120740; E-mail: lha{at}phys.au.dk.

The absorption spectra of two photoactive yellow protein model chromophores have been measured in vacuum using an electrostatic ion storage ring. The absorption spectrum of the isolated chromophore is an important reference for deducing the influence of the protein environment on the electronic energy levels of the chromophore and separating the intrinsic properties of the chromophore from properties induced by the protein environment. In vacuum the deprotonated trans-thiophenyl-p-coumarate model chromophore has an absorption maximum at 460 nm, whereas the photoactive yellow protein absorbs maximally at 446 nm. The protein environment thus only slightly blue-shifts the absorption. In contrast, the absorption of the model chromophore in aqueous solution is significantly blue-shifted (_max = 395 nm). A deprotonated trans-p-coumaric acid has also been studied to elucidate the effect of thioester formation and phenol deprotonation. The sum of these two changes on the chromophore induces a red shift both in vacuum and in aqueous solution.

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