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1 November 2006 Analogue Chromophore Study of the Influence of Electronic Perturbation on Color Regulation of Photoactive Yellow Protein
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Abstract

We report a unique λmax shift of the absorption maximum of a photoactive yellow protein (PYP) analogue reconstituted with a fluorinated chromophore (F-PYP). The difference in λmax between the free chromophore and the protein was significantly larger than that with the native chromophore. We concluded that the unusual λmax shift is caused by the electronegative character of the fluorine atom and not by steric hindrance. This result suggests that formation of a hydrogen bond between the fluorine atom and one or more amino acid residues could neutralize its electron-withdrawing character. The properties of analogues of PYP with brominated and methylated chromophore could be explained as an effect of steric hindrance.

Hiroshi Yamada, Masato Kumauchi, Norio Hamada, Xiang-Guo Zheng, Il Ho Park, Katsuyoshi Masuda, Kazuo Yoshihara, and Fumio Tokunaga "Analogue Chromophore Study of the Influence of Electronic Perturbation on Color Regulation of Photoactive Yellow Protein," Photochemistry and Photobiology 82(6), 1422-1425, (1 November 2006). https://doi.org/10.1562/2006-01-17-RA-781
Received: 12 January 2006; Accepted: 1 May 2006; Published: 1 November 2006
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