Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain

Maeda, Masahiro; Hamada, Daizo; Hoshino, Masaru; Onda, Yayoi; Hase, Toshiharu; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M112002200

アクセス数:313件（2025-01-29 02:04 集計）

固定URL: https://hdl.handle.net/11094/71303

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タイトル	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
著者	著者名 Maeda, Masahiro
	NRID 1000060372132 1000060372132 著者名 Hamada, Daizo
	NRID 1000070304053 1000070304053 著者名 Hoshino, Masaru
	NRID 1000070368463 1000070368463 著者名 Onda, Yayoi
	NRID 1000000127276 1000000127276 著者名 Hase, Toshiharu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Masahiro Maeda, Daizo Hamada, Masaru Hoshino, Yayoi Onda, Toshiharu Hase and Yuji Goto. Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain. J. Biol. Chem. 2002; 277, 17101-17107. © the American Society for Biochemistry and Molecular Biology
抄録	Maize ferredoxin-NADP+reductase (FNR) consists of flavin adenine dinucleotide (FAD) and NADP+ binding domains with a FAD molecule bound noncovalently in the cleft between these domains. The structural changes of FNR induced by dissociation of FAD have been characterized by a combination of optical and biochemical methods. The CD spectrum of the FAD-depleted FNR (apo-FNR) suggested that removal of FAD from holo-FNR produced an intermediate conformational state with partially disrupted secondary and tertiary structures. Small angle x-ray scattering indicated that apo-FNR assumes a conformation that is less globular in comparison with holo-FNR but is not completely chain-like. Interestingly, the replacement of tyrosine 95 responsible for FAD binding with alanine resulted in a molecular form similar to apo-protein of the wild-type enzyme. Both apo- and Y95A-FNR species bound to Cibacron Blue affinity resin, indicating the presence of a native-like conformation for the NADP+ binding domain. On the other hand, no evidence was found for the existence of folded conformations in the FAD binding domains of these proteins. These results suggested that FAD-depleted FNR assumes a partially folded structure with a residual NADP+ binding domain but a disordered FAD binding domain.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	277(19)
ページ	17101-17107
刊行年月	2002-05
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71303
eISSN	1083351X
NCID	AA1202472X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M112002200
アクセス権	open access
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2002, 277(19), p. 17101-17107
DC.title	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
DC.creator	Maeda, Masahiro
	Hamada, Daizo
	Hoshino, Masaru
	Onda, Yayoi
	Hase, Toshiharu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2002-05
DC.identifier	https://doi.org/10.1074/jbc.M112002200
DC.description	This research was originally published in the Journal of Biological Chemistry. Masahiro Maeda, Daizo Hamada, Masaru Hoshino, Yayoi Onda, Toshiharu Hase and Yuji Goto. Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain. J. Biol. Chem. 2002; 277, 17101-17107. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Maize ferredoxin-NADP+reductase (FNR) consists of flavin adenine dinucleotide (FAD) and NADP+ binding domains with a FAD molecule bound noncovalently in the cleft between these domains. The structural changes of FNR induced by dissociation of FAD have been characterized by a combination of optical and biochemical methods. The CD spectrum of the FAD-depleted FNR (apo-FNR) suggested that removal of FAD from holo-FNR produced an intermediate conformational state with partially disrupted secondary and tertiary structures. Small angle x-ray scattering indicated that apo-FNR assumes a conformation that is less globular in comparison with holo-FNR but is not completely chain-like. Interestingly, the replacement of tyrosine 95 responsible for FAD binding with alanine resulted in a molecular form similar to apo-protein of the wild-type enzyme. Both apo- and Y95A-FNR species bound to Cibacron Blue affinity resin, indicating the presence of a native-like conformation for the NADP+ binding domain. On the other hand, no evidence was found for the existence of folded conformations in the FAD binding domains of these proteins. These results suggested that FAD-depleted FNR assumes a partially folded structure with a residual NADP+ binding domain but a disordered FAD binding domain.
DC.format	71303
citation_title	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
citation_author	Maeda, Masahiro
	Hamada, Daizo
	Hoshino, Masaru
	Onda, Yayoi
	Hase, Toshiharu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2002-05
citation_journal_title	Journal of Biological Chemistry
citation_volume	277
citation_issue	19
citation_firstpage	17101
citation_lastpage	17107
citation_doi	https://doi.org/10.1074/jbc.M112002200
citation_public_url	https://hdl.handle.net/11094/71303

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