Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom

Mizuno, Misao; Sato, Keita; Yamashita, Takahiro; Sakai, Kazumi; Imamoto, Yasushi; Yamano, Yumiko; Wada, Akimori; Ohuchi, Hideyo; Shichida, Yoshinori; Mizutani, Yasuhisa

doi:https://doi.org/10.1021/acs.jpcb.2c08780

Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom

Mizuno, Misao; Sato, Keita; Yamashita, Takahiro et al.

Journal of Physical Chemistry B, 2023, 127(10), 2169-2176

Number of Access:1,005（2025-09-10 12:27 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/91286

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Title	Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom
Creator	NRID 1000010464257 1000010464257 CreatorName Mizuno, Misao
	NRID 1000080725622 1000080725622 CreatorName Sato, Keita
	NRID 1000050378535 1000050378535 CreatorName Yamashita, Takahiro
	CreatorName Sakai, Kazumi
	NRID 1000080263200 1000080263200 CreatorName Imamoto, Yasushi
	NRID 1000050208831 1000050208831 CreatorName Yamano, Yumiko
	NRID 1000080158683 1000080158683 CreatorName Wada, Akimori
	NRID 1000000253229 1000000253229 CreatorName Ohuchi, Hideyo
	NRID 1000060127090 1000060127090 CreatorName Shichida, Yoshinori
	NRID 1000060270469 1000060270469 ORCID 0000-0002-3754-5720 0000-0002-3754-5720 researchmap permalink read0182663 read0182663 Scopus Author ID 7202969842 7202969842 CreatorName Mizutani, Yasuhisa
Description	Misao Mizuno, Keita Sato, Takahiro Yamashita, Kazumi Sakai, Yasushi Imamoto, Yumiko Yamano, Akimori Wada, Hideyo Ohuchi, Yoshinori Shichida, and Yasuhisa Mizutani, Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom, The Journal of Physical Chemistry B, 127(10), 2169-2176, March 16, 2023, © 2023 American Chemical Society. DOI: 10.1021/acs.jpcb.2c08780
Abstract	Opsins are photosensitive G protein-coupled receptor proteins and are classified into visual and nonvisual receptors. Opn5L1 is a nonvisual opsin that binds all-trans retinal as a chromophore. A unique feature of Opn5L1 is that the protein exhibits a photocyclic reaction upon photoexcitation. Determining the chromophore structures of intermediates in the photocycle is essential for understanding the functional mechanism of Opn5L1. A previous study revealed that a long-lived intermediate in the photocycle cannot activate the G protein and forms a covalent bond between the retinal chromophore and a nearby cysteine residue. However, the position of this covalent bond in the chromophore remains undetermined. Here, we report a resonance Raman study on isotopically labeled samples in combination with density functional theory calculations and reveal that the 11th carbon atom of the chromophore of the intermediate forms a covalent linkage to the cysteine residue. Furthermore, vibrational assignments based on the isotopic substitutions and density functional theory calculations suggested that the Schiff base of the intermediate is deprotonated. The chromophore structure determined in the present study well explains the mechanism of the photocyclic reaction, which is crucial to the photobiological function of Opn5L1.
Publisher	American Chemical Society
Source Title	Journal of Physical Chemistry B
Volume (Issue)	127(10)
Page	2169-2176
Date of Issued	2023-03-16
Language	English
Handle URL	https://hdl.handle.net/11094/91286
PISSN	15206106
eISSN	15205207
Relation.isVersionOf	DOI (Publisher Version) https://doi.org/10.1021/acs.jpcb.2c08780
Access Rights	open access
CopyRight	This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jpcb.2c08780.
oaire:version	Accepted Manuscript
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Physical Chemistry B. 2023, 127(10), p. 2169-2176
DC.title	Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom
DC.creator	Mizuno, Misao
	Sato, Keita
	Yamashita, Takahiro
	Sakai, Kazumi
	Imamoto, Yasushi
	Yamano, Yumiko
	Wada, Akimori
	Ohuchi, Hideyo
	Shichida, Yoshinori
	Mizutani, Yasuhisa
DC.publisher	American Chemical Society
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2023-03-16
DC.identifier	https://doi.org/10.1021/acs.jpcb.2c08780
DC.description	Misao Mizuno, Keita Sato, Takahiro Yamashita, Kazumi Sakai, Yasushi Imamoto, Yumiko Yamano, Akimori Wada, Hideyo Ohuchi, Yoshinori Shichida, and Yasuhisa Mizutani, Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom, The Journal of Physical Chemistry B, 127(10), 2169-2176, March 16, 2023, © 2023 American Chemical Society. DOI: 10.1021/acs.jpcb.2c08780
DCTERMS.abstract	Opsins are photosensitive G protein-coupled receptor proteins and are classified into visual and nonvisual receptors. Opn5L1 is a nonvisual opsin that binds all-trans retinal as a chromophore. A unique feature of Opn5L1 is that the protein exhibits a photocyclic reaction upon photoexcitation. Determining the chromophore structures of intermediates in the photocycle is essential for understanding the functional mechanism of Opn5L1. A previous study revealed that a long-lived intermediate in the photocycle cannot activate the G protein and forms a covalent bond between the retinal chromophore and a nearby cysteine residue. However, the position of this covalent bond in the chromophore remains undetermined. Here, we report a resonance Raman study on isotopically labeled samples in combination with density functional theory calculations and reveal that the 11th carbon atom of the chromophore of the intermediate forms a covalent linkage to the cysteine residue. Furthermore, vibrational assignments based on the isotopic substitutions and density functional theory calculations suggested that the Schiff base of the intermediate is deprotonated. The chromophore structure determined in the present study well explains the mechanism of the photocyclic reaction, which is crucial to the photobiological function of Opn5L1.
DC.rights	This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jpcb.2c08780.
DC.format	91286
citation_title	Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom
citation_author	Mizuno, Misao
	Sato, Keita
	Yamashita, Takahiro
	Sakai, Kazumi
	Imamoto, Yasushi
	Yamano, Yumiko
	Wada, Akimori
	Ohuchi, Hideyo
	Shichida, Yoshinori
	Mizutani, Yasuhisa
citation_publisher	American Chemical Society
citation_language	English
citation_date	2023-03-16
citation_journal_title	Journal of Physical Chemistry B
citation_volume	127
citation_issue	10
citation_firstpage	2169
citation_lastpage	2176
citation_doi	https://doi.org/10.1021/acs.jpcb.2c08780
citation_public_url	https://hdl.handle.net/11094/91286

Chromophore Structure in an Inactive State of a Novel Photosensor Protein Opn5L1: Resonance Raman Evidence for the Formation of a Deprotonated Adduct at the 11th Carbon Atom

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