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

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

Maeda, Masahiro; Hamada, Daizo; Hoshino, Masaru et al.

Journal of Biological Chemistry, 2002, 277(19), 17101-17107

Number of Access:645（2025-08-30 13:29 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71303

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Title	Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain
Creator	CreatorName Maeda, Masahiro
	NRID 1000060372132 1000060372132 CreatorName Hamada, Daizo
	NRID 1000070304053 1000070304053 CreatorName Hoshino, Masaru
	NRID 1000070368463 1000070368463 CreatorName Onda, Yayoi
	NRID 1000000127276 1000000127276 CreatorName Hase, Toshiharu
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 CreatorName Goto, Yuji
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
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.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	277(19)
Page	17101-17107
Date of Issued	2002-05
Language	English
Handle URL	https://hdl.handle.net/11094/71303
eISSN	1083351X
NCID	AA1202472X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M112002200
Access Rights	open access
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. 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	English
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	English
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

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

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