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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Autori principali: Roy, Partha Pratim (Autore) , Buckup, Tiago (Autore)
Natura: Article (Journal)
Lingua:inglese
Pubblicazione: February 11, 2019
In: The journal of physical chemistry letters
Year: 2019, Volume: 10, Fascicolo: 5, Pages: 1012-1017
ISSN:1948-7185
DOI:10.1021/acs.jpclett.8b03805
Accesso online:Verlag, Volltext: https://doi.org/10.1021/acs.jpclett.8b03805
Testo
Note sull'autore:Partha Pratim Roy, Rei Abe-Yoshizumi, Hideki Kandori, and Tiago Buckup
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Riassunto: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.
Descrizione del documento:Gesehen am 29.04.2019
Descrizione fisica:Online Resource
ISSN:1948-7185
DOI:10.1021/acs.jpclett.8b03805