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• W2913373374 endingPage "1017" @default.
• W2913373374 startingPage "1012" @default.
• W2913373374 abstract "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." @default.
• W2913373374 created "2019-02-21" @default.
• W2913373374 creator A5007870329 @default.
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• W2913373374 creator A5082839273 @default.
• W2913373374 date "2019-02-11" @default.
• W2913373374 modified "2023-09-24" @default.
• W2913373374 title "Point Mutation of <i>Anabaena</i> Sensory Rhodopsin Enhances Ground-State Hydrogen Out-of-Plane Wag Raman Activity" @default.
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• W2913373374 doi "https://doi.org/10.1021/acs.jpclett.8b03805" @default.
• W2913373374 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30742765" @default.
• W2913373374 hasPublicationYear "2019" @default.
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