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Analogue Chromophore Study of the Influence of Electronic Perturbation on Color Regulation of Photoactive Yellow Proteint †
Author(s) -
Yamada Hiroshi,
Kumauchi Masato,
Hamada Norio,
Zheng XiangGuo,
Park II Ho,
Masuda Katsuyoshi,
Yoshihara Kazuo,
Tokunaga Fumio
Publication year - 2006
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.2006.tb09794.x
Subject(s) - chromophore , steric effects , chemistry , photochemistry , hydrogen bond , fluorine , polar effect , hydrogen atom , stereochemistry , molecule , organic chemistry , alkyl
We report a unique Λ Amax shift of the absorption maximum of a photoactive yellow protein (PYP) analogue reconstituted with a fluorinated chromophore (F‐PYP). The difference in Λ Amax between the free chromophore and the protein was significantly larger than that with the native chromophore. We concluded that the unusual Λ Amax 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.