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Spectroscopic ruler for measuring active-site distortions based on Raman optical activity of a hydrogen out-of-plane vibration

発表形態:
原著論文
主要業績:
単著・共著:
発表年月:
2018年01月
DOI:
10.1073/pnas.1806491115
会議属性:
査読:
リンク情報:

日本語フィールド

著者:
Haraguchi, Shojiro; Shingae, Takahito; Fujisawa, Tomotsumi; Kasai, Noritaka; Kumauchi, Masato; Hanamoto, Takeshi; Hoff, Wouter D.; Unno, Masashi
題名:
Spectroscopic ruler for measuring active-site distortions based on Raman optical activity of a hydrogen out-of-plane vibration
発表情報:
Proceedings of the National Academy of Sciences of the United States of America 巻: 115 号: 35 ページ: 8671 - 8675
キーワード:
概要:
Photoactive yellow protein (PYP), from the phototrophic bacterium Halorhodospira halophila, is a small water-soluble photoreceptor protein and contains p-coumaric acid (pCA) as a chromophore. PYP has been an attractive model for studying the physical chemistry of protein active sites. Here, we explore how Raman optical activity (ROA) can be used to extract quantitative information on distortions of the pCA chromophore at the active site in PYP. We use13C8-pCA to assign an intense signal at 826 cm−1 in the ROA spectrum of PYP to a hydrogen out-of-plane vibration of the ethylenic moiety of the chromophore. Quantum-chemical calculations based on density functional theory demonstrate that the sign of this ROA band reports the direction of the distortion in the dihedral angle about the ethylenic C=C bond, while its amplitude is proportional to the dihedral angle. These results document the ability of ROA to quantify structural deformations of a cofactor molecule embedded in a protein moiety.
抄録:

英語フィールド

Author:
Haraguchi, Shojiro; Shingae, Takahito; Fujisawa, Tomotsumi; Kasai, Noritaka; Kumauchi, Masato; Hanamoto, Takeshi; Hoff, Wouter D.; Unno, Masashi
Title:
Spectroscopic ruler for measuring active-site distortions based on Raman optical activity of a hydrogen out-of-plane vibration
Announcement information:
Proceedings of the National Academy of Sciences of the United States of America Vol: 115 Issue: 35 Page: 8671 - 8675
An abstract:
Photoactive yellow protein (PYP), from the phototrophic bacterium Halorhodospira halophila, is a small water-soluble photoreceptor protein and contains p-coumaric acid (pCA) as a chromophore. PYP has been an attractive model for studying the physical chemistry of protein active sites. Here, we explore how Raman optical activity (ROA) can be used to extract quantitative information on distortions of the pCA chromophore at the active site in PYP. We use13C8-pCA to assign an intense signal at 826 cm−1 in the ROA spectrum of PYP to a hydrogen out-of-plane vibration of the ethylenic moiety of the chromophore. Quantum-chemical calculations based on density functional theory demonstrate that the sign of this ROA band reports the direction of the distortion in the dihedral angle about the ethylenic C=C bond, while its amplitude is proportional to the dihedral angle. These results document the ability of ROA to quantify structural deformations of a cofactor molecule embedded in a protein moiety.


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