Exploring the Active Site Structure of a Photoreceptor Protein by Raman Optical Activity
| Autor: | Takashi Kikukawa, Masato Kumauchi, Masashi Unno, Naoki Kamo |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Halobacterium salinarum
Models Molecular biology Spectrometer Chemistry Analytical chemistry Active site Photoreceptor protein Bacteriorhodopsin Chromophore Spectrum Analysis Raman Photochemistry Surfaces Coatings and Films symbols.namesake Bacteriorhodopsins Catalytic Domain Excited state Materials Chemistry symbols biology.protein Raman optical activity Physical and Theoretical Chemistry Raman spectroscopy |
| Zdroj: | The Journal of Physical Chemistry B. 117:1321-1325 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/jp4001187 |
| Popis: | We have developed a near-infrared excited Raman optical activity (ROA) spectrometer and report the first measurement of near-infrared ROA spectra of a light-driven proton pump, bacteriorhodopsin. Our results demonstrate that a near-infrared excitation enables us to measure the ROA spectra of the chromophore within a protein environment. Furthermore, the ROA spectra of the all-trans, 15-anti and 13-cis, 15-syn isomers differ significantly, indicating a high structural sensitivity of the ROA spectra. We therefore expect that future applications of the near-infrared ROA will allow the experimental elucidation of the active site structures in other proteins as well as reaction intermediates. |
| Databáze: | OpenAIRE |
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