Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115, Issue 35, Pages 8671-8675Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1806491115
Keywords
photoreceptor; chromophore; vibrational spectroscopy; density functional theory; molecular strain
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Funding
- Japan Society for the Promotion of Science KAKENHI [17K05756, 16K17859]
- National Science Foundation [CHE-1413739]
- Grants-in-Aid for Scientific Research [17K05756, 16K17859] Funding Source: KAKEN
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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 use (13)C8-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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