Low-temperature FTIR spectroscopy of the L/Q switch of proteorhodopsin-Reference-Cited by-同舟云学术

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Low-temperature FTIR spectroscopy of the L/Q switch of proteorhodopsin

Published:2024 Issue:35 Volume:26 Page:22959-22967
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Nishikino Tatsuro¹²,Sugimoto Teppei¹,Kandori Hideki¹²^ORCID

Affiliation:

1. Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan

2. OptoBioTechnology Research Center, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan

Abstract

Low-temperature FTIR spectroscopy of L105Q GPR monitored the conversion of the GPR structure into a BPR structure in terms of the local environments of the retinal chromophore, by which color is converted known as the L/Q switch.

Funder

Ministry of Education, Culture, Sports, Science and Technology

Japan Science and Technology Agency

Japan Society for the Promotion of Science

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CP/D4CP02248C

Reference55 articles.

1. Microbial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms

2. Of ion pumps, sensors and channels — Perspectives on microbial rhodopsins between science and history

3. Eubacterial rhodopsins — Unique photosensors and diverse ion pumps

4. Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications

5. Protonation-state-Coupled Conformational Dynamics in Reaction Mechanisms of Channel and Pump Rhodopsins

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