Analogue Chromophore Study of the Influence of Electronic Perturbation on Color Regulation of Photoactive Yellow Protein
| Autor: | Masato Kumauchi, Norio Hamada, Kazuo Yoshihara, Katsuyoshi Masuda, Fumio Tokunaga, Hiroshi Yamada, Il Ho Park, Xiang-Guo Zheng |
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| Rok vydání: | 2006 |
| Předmět: |
Photoactive yellow protein
Steric effects Stereochemistry Hydrogen bond Color chemistry.chemical_element General Medicine Hydrogen-Ion Concentration Chromophore Photoreceptors Microbial Photochemistry Electrochemistry Biochemistry Bacterial Proteins chemistry Spectrophotometry Fluorine Spectrophotometry Ultraviolet Amino acid residue Physical and Theoretical Chemistry |
| Zdroj: | Photochemistry and Photobiology. 82:1422-1425 |
| ISSN: | 1751-1097 0031-8655 |
| Popis: | We report a unique lambdamax shift of the absorption maximum of a photoactive yellow protein (PYP) analogue reconstituted with a fluorinated chromophore (F-PYP). The difference in lambdamax between the free chromophore and the protein was significantly larger than that with the native chromophore. We concluded that the unusual lambdamax 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. |
| Databáze: | OpenAIRE |
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