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Raman Optical Activity Reveals Carotenoid Photoactivation Events in the Orange Carotenoid Protein in Solution

発表形態:
原著論文
主要業績:
単著・共著:
発表年月:
2017年08月
DOI:
10.1021/jacs.7b05193
会議属性:
査読:
リンク情報:

日本語フィールド

著者:
Fujisawa, Tomotsumi; Leverenz, Ryan L.; Leverenz, Ryan L.; Leverenz, Ryan L.; Nagamine, Momoka; Kerfeld, Cheryl A.; Kerfeld, Cheryl A.; Unno, Masashi
題名:
Raman Optical Activity Reveals Carotenoid Photoactivation Events in the Orange Carotenoid Protein in Solution
発表情報:
Journal of the American Chemical Society 巻: 139 号: 30 ページ: 10456 - 10460
キーワード:
概要:
© 2017 American Chemical Society. The orange carotenoid protein (OCP) plays an important role in photoprotection in cyanobacteria, which is achieved by the photoconversion from the orange dark state (OCP O ) to the red active state (OCP R ). Using Raman optical activity (ROA), we studied the conformations of the carotenoid chromophore in the active sites of OCP O and OCP R . This ROA measurement directly observed the chromophore conformation of native OCP in solution, and th e measurement of OCP R first demonstrated the ROA spectroscopy for the transient species. For OCP O , the spectral features of ROA were mostly reproduced by the quantum chemical calculation based on the crystal structure of the OCP. Within the spatial resolution (∼2 Å), a slight modification of the polyene-chain distortion improved the agreement between the observed and calculated ROA spectra. While the crystal structure of OCP R is not available, the ROA spectrum of OCP R was reproduced by using the crystal structure of red carotenoid protein (RCP), an OCP R proxy. The present results showed that the chromophore conformations in the crystal structures of OCP and RCP hold true for OCP O and OCP R in solution. Particularly, ROA spectroscopy of the native OCP R provides a direct support for the 12 Å translocation of chromophore in the photoactivation, which was proposed by X-ray crystallography using RCP [R. L. Leverenz, M. Sutter, et al. Science 2015, 348, 1463-1466].
抄録:

英語フィールド

Author:
Fujisawa, Tomotsumi; Leverenz, Ryan L.; Leverenz, Ryan L.; Leverenz, Ryan L.; Nagamine, Momoka; Kerfeld, Cheryl A.; Kerfeld, Cheryl A.; Unno, Masashi
Title:
Raman Optical Activity Reveals Carotenoid Photoactivation Events in the Orange Carotenoid Protein in Solution
Announcement information:
Journal of the American Chemical Society Vol: 139 Issue: 30 Page: 10456 - 10460
An abstract:
© 2017 American Chemical Society. The orange carotenoid protein (OCP) plays an important role in photoprotection in cyanobacteria, which is achieved by the photoconversion from the orange dark state (OCP O ) to the red active state (OCP R ). Using Raman optical activity (ROA), we studied the conformations of the carotenoid chromophore in the active sites of OCP O and OCP R . This ROA measurement directly observed the chromophore conformation of native OCP in solution, and th e measurement of OCP R first demonstrated the ROA spectroscopy for the transient species. For OCP O , the spectral features of ROA were mostly reproduced by the quantum chemical calculation based on the crystal structure of the OCP. Within the spatial resolution (∼2 Å), a slight modification of the polyene-chain distortion improved the agreement between the observed and calculated ROA spectra. While the crystal structure of OCP R is not available, the ROA spectrum of OCP R was reproduced by using the crystal structure of red carotenoid protein (RCP), an OCP R proxy. The present results showed that the chromophore conformations in the crystal structures of OCP and RCP hold true for OCP O and OCP R in solution. Particularly, ROA spectroscopy of the native OCP R provides a direct support for the 12 Å translocation of chromophore in the photoactivation, which was proposed by X-ray crystallography using RCP [R. L. Leverenz, M. Sutter, et al. Science 2015, 348, 1463-1466].


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