Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein

Horigome, Daisuke; Satoh, Hiroyuki; Itoh, Nobue; Mitsunaga, Katsuyoshi; Oonishi, Isao; Nakagawa, Atushi; Uchida, Akira

doi:https://doi.org/10.1074/jbc.M609458200

Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein

Horigome, Daisuke; Satoh, Hiroyuki; Itoh, Nobue et al.

Journal of Biological Chemistry, 2007, 282(9), 6525-6531

Number of Access:835（2025-08-14 00:15 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73654

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Title	Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein
Creator	CreatorName Horigome, Daisuke
	NRID 1000080187228 1000080187228 CreatorName Satoh, Hiroyuki
	CreatorName Itoh, Nobue
	CreatorName Mitsunaga, Katsuyoshi
	CreatorName Oonishi, Isao
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 CreatorName Nakagawa, Atushi
	NRID 1000030176680 1000030176680 CreatorName Uchida, Akira
Description	This research was originally published in Journal of Biological Chemistry. Daisuke Horigome, Hiroyuki Satoh, Nobue Itoh, Katsuyoshi Mitsunaga, Isao Oonishi, Atsushi Nakagawa and Akira Uchida. Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein. Journal of Biological Chemistry. 2007; 282, 6525-6531. © the American Society for Biochemistry and Molecular Biology.
Abstract	A water-soluble chlorophyll-binding protein (WSCP) is the single known instance of a putative chlorophyll (Chl) carrier in green plants. Recently the photoprotective function of WSCP has been demonstrated by EPR measurements; the light-induced singlet-oxygen formation of Chl in the WSCP tetramer is about four times lower than that of unbound Chl. This paper describes the crystal structure of the WSCP-Chl complex purified from leaves of Lepidium virginicum (Virginia pepperweed) to clarify the mechanism of its photoprotective function. The WSCP-Chl complex is a homotetramer comprising four protein chains of 180 amino acids and four Chl molecules. At the center of the complex one hydrophobic cavity is formed in which all of the four Chl molecules are tightly packed and isolated from bulk solvent. With reference to the novel Chl-binding mode, we propose that the photoprotection mechanism may be based on the inhibition of physical contact between the Chl molecules and molecular oxygen.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	282(9)
Page	6525-6531
Date of Issued	2007-03
Language	English
Handle URL	https://hdl.handle.net/11094/73654
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M609458200
Relation.isIdenticalTo	PMID 17170107
Access Rights	open access
CopyRight	© the American Society for Biochemistry and Molecular Biology.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2007, 282(9), p. 6525-6531
DC.title	Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein
DC.creator	Horigome, Daisuke
	Satoh, Hiroyuki
	Itoh, Nobue
	Mitsunaga, Katsuyoshi
	Oonishi, Isao
	Nakagawa, Atushi
	Uchida, Akira
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2007-03
DC.identifier	https://doi.org/10.1074/jbc.M609458200
DC.description	This research was originally published in Journal of Biological Chemistry. Daisuke Horigome, Hiroyuki Satoh, Nobue Itoh, Katsuyoshi Mitsunaga, Isao Oonishi, Atsushi Nakagawa and Akira Uchida. Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein. Journal of Biological Chemistry. 2007; 282, 6525-6531. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	A water-soluble chlorophyll-binding protein (WSCP) is the single known instance of a putative chlorophyll (Chl) carrier in green plants. Recently the photoprotective function of WSCP has been demonstrated by EPR measurements; the light-induced singlet-oxygen formation of Chl in the WSCP tetramer is about four times lower than that of unbound Chl. This paper describes the crystal structure of the WSCP-Chl complex purified from leaves of Lepidium virginicum (Virginia pepperweed) to clarify the mechanism of its photoprotective function. The WSCP-Chl complex is a homotetramer comprising four protein chains of 180 amino acids and four Chl molecules. At the center of the complex one hydrophobic cavity is formed in which all of the four Chl molecules are tightly packed and isolated from bulk solvent. With reference to the novel Chl-binding mode, we propose that the photoprotection mechanism may be based on the inhibition of physical contact between the Chl molecules and molecular oxygen.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
DC.format	73654
citation_title	Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein
citation_author	Horigome, Daisuke
	Satoh, Hiroyuki
	Itoh, Nobue
	Mitsunaga, Katsuyoshi
	Oonishi, Isao
	Nakagawa, Atushi
	Uchida, Akira
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2007-03
citation_journal_title	Journal of Biological Chemistry
citation_volume	282
citation_issue	9
citation_firstpage	6525
citation_lastpage	6531
citation_doi	https://doi.org/10.1074/jbc.M609458200
citation_pmid	17170107
citation_public_url	https://hdl.handle.net/11094/73654

Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein

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