Exploring the active site structure of a photoreceptor protein by Raman optical activity.

Masashi Unno, Takashi Kikukawa, Masato Kumauchi, Naoki Kamo

Department of Chemistry and Applied Chemistry, Graduate School of Science and Engineering, Saga University, Saga 840-8502, Japan. unno@cc.saga-u.ac.jp

The journal of physical chemistry. B 2013 Feb 7

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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.

Citation

Masashi Unno, Takashi Kikukawa, Masato Kumauchi, Naoki Kamo. Exploring the active site structure of a photoreceptor protein by Raman optical activity. The journal of physical chemistry. B. 2013 Feb 7;117(5):1321-5