Point mutation of Anabaena sensory rhodopsin Enhances ground-state hydrogen out-of-plane wag Raman activity
The interaction between the retinal protonated Schiff base (RPSB) and surrounding protein residues inside the retinal pocket is believed to play a major role in the ultrafast isomerization of the former. Coherent time-resolved vibrational spectroscopic techniques are applied to reveal the effect of...
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| Main Authors: | , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
February 11, 2019
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| In: |
The journal of physical chemistry letters
Year: 2019, Volume: 10, Issue: 5, Pages: 1012-1017 |
| ISSN: | 1948-7185 |
| DOI: | 10.1021/acs.jpclett.8b03805 |
| Online Access: | Verlag, Volltext: https://doi.org/10.1021/acs.jpclett.8b03805
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| Author Notes: | Partha Pratim Roy, Rei Abe-Yoshizumi, Hideki Kandori, and Tiago Buckup |
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| 520 | |a The interaction between the retinal protonated Schiff base (RPSB) and surrounding protein residues inside the retinal pocket is believed to play a major role in the ultrafast isomerization of the former. Coherent time-resolved vibrational spectroscopic techniques are applied to reveal the effect of changes in the protein architecture by point mutations (V112N and L83Q) close to the RPSB in Anabaena sensory rhodopsin (ASR). Our study reveals that such point mutations have a minor effect on the low-frequency (<400 cm-1) torsional modes but dramatically influence the ground-state vibrational Raman activity of the C14-H out-of-plane (HOOP) wag mode (800-820 cm-1). In mutated ASR, the increase of HOOP Raman activity in the ground state is experimentally observed for the all-trans RPSB, which has shorter excited-state lifetime than in wild-type ASR. This indicates that predistortion of the RPSB inside the mutated retinal pocket is a major factor in the acceleration of the isomerization rate. | ||
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