Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy

Abstract Protein-bound water molecules are essential for the structure and function of many membrane proteins, including G-protein-coupled receptors (GPCRs). Our prior work focused on studying the primate green- (MG) and red- (MR) sensitive visual pigments using low-temperature Fourier transform inf...

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Autores principales:	Kota Katayama, Yuki Nonaka, Kei Tsutsui, Hiroo Imai, Hideki Kandori
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2eccd9a414a540d2a63ffd2a3bd85d9d
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spelling	oai:doaj.org-article:2eccd9a414a540d2a63ffd2a3bd85d9d2021-12-02T12:32:50ZSpectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy10.1038/s41598-017-05177-42045-2322https://doaj.org/article/2eccd9a414a540d2a63ffd2a3bd85d9d2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05177-4https://doaj.org/toc/2045-2322Abstract Protein-bound water molecules are essential for the structure and function of many membrane proteins, including G-protein-coupled receptors (GPCRs). Our prior work focused on studying the primate green- (MG) and red- (MR) sensitive visual pigments using low-temperature Fourier transform infrared (FTIR) spectroscopy, which revealed protein-bound waters in both visual pigments. Although the internal waters are located in the vicinity of both the retinal Schiff base and retinal β-ionone ring, only the latter showed differences between MG and MR, which suggests their role in color tuning. Here, we report FTIR spectra of primate blue-sensitive pigment (MB) in the entire mid-IR region, which reveal the presence of internal waters that possess unique water vibrational signals that are reminiscent of a water cluster. These vibrational signals of the waters are influenced by mutations at position Glu113 and Trp265 in Rh, which suggest that these waters are situated between these two residues. Because Tyr265 is the key residue for achieving the spectral blue-shift in λmax of MB, we propose that these waters are responsible for the increase in polarity toward the retinal Schiff base, which leads to the localization of the positive charge in the Schiff base and consequently causes the blue-shift of λmax.Kota KatayamaYuki NonakaKei TsutsuiHiroo ImaiHideki KandoriNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kota Katayama Yuki Nonaka Kei Tsutsui Hiroo Imai Hideki Kandori Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy
description	Abstract Protein-bound water molecules are essential for the structure and function of many membrane proteins, including G-protein-coupled receptors (GPCRs). Our prior work focused on studying the primate green- (MG) and red- (MR) sensitive visual pigments using low-temperature Fourier transform infrared (FTIR) spectroscopy, which revealed protein-bound waters in both visual pigments. Although the internal waters are located in the vicinity of both the retinal Schiff base and retinal β-ionone ring, only the latter showed differences between MG and MR, which suggests their role in color tuning. Here, we report FTIR spectra of primate blue-sensitive pigment (MB) in the entire mid-IR region, which reveal the presence of internal waters that possess unique water vibrational signals that are reminiscent of a water cluster. These vibrational signals of the waters are influenced by mutations at position Glu113 and Trp265 in Rh, which suggest that these waters are situated between these two residues. Because Tyr265 is the key residue for achieving the spectral blue-shift in λmax of MB, we propose that these waters are responsible for the increase in polarity toward the retinal Schiff base, which leads to the localization of the positive charge in the Schiff base and consequently causes the blue-shift of λmax.
format	article
author	Kota Katayama Yuki Nonaka Kei Tsutsui Hiroo Imai Hideki Kandori
author_facet	Kota Katayama Yuki Nonaka Kei Tsutsui Hiroo Imai Hideki Kandori
author_sort	Kota Katayama
title	Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy
title_short	Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy
title_full	Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy
title_fullStr	Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy
title_full_unstemmed	Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy
title_sort	spectral tuning mechanism of primate blue-sensitive visual pigment elucidated by ftir spectroscopy
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/2eccd9a414a540d2a63ffd2a3bd85d9d
work_keys_str_mv	AT kotakatayama spectraltuningmechanismofprimatebluesensitivevisualpigmentelucidatedbyftirspectroscopy AT yukinonaka spectraltuningmechanismofprimatebluesensitivevisualpigmentelucidatedbyftirspectroscopy AT keitsutsui spectraltuningmechanismofprimatebluesensitivevisualpigmentelucidatedbyftirspectroscopy AT hirooimai spectraltuningmechanismofprimatebluesensitivevisualpigmentelucidatedbyftirspectroscopy AT hidekikandori spectraltuningmechanismofprimatebluesensitivevisualpigmentelucidatedbyftirspectroscopy
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Spectral Tuning Mechanism of Primate Blue-sensitive Visual Pigment Elucidated by FTIR Spectroscopy

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