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http://purl.uniprot.org/citations/17611542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17611542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17611542http://www.w3.org/2000/01/rdf-schema#comment"Oxygen-evolving photosynthetic organisms regulate carbon metabolism through a light-dependent redox signalling pathway. Electrons are shuttled from photosystem I by means of ferredoxin (Fdx) to ferredoxin-thioredoxin reductase (FTR), which catalyses the two-electron-reduction of chloroplast thioredoxins (Trxs). These modify target enzyme activities by reduction, regulating carbon flow. FTR is unique in its use of a [4Fe-4S] cluster and a proximal disulphide bridge in the conversion of a light signal into a thiol signal. We determined the structures of FTR in both its one- and its two-electron-reduced intermediate states and of four complexes in the pathway, including the ternary Fdx-FTR-Trx complex. Here we show that, in the first complex (Fdx-FTR) of the pathway, the Fdx [2Fe-2S] cluster is positioned suitably for electron transfer to the FTR [4Fe-4S] centre. After the transfer of one electron, an intermediate is formed in which one sulphur atom of the FTR active site is free to attack a disulphide bridge in Trx and the other sulphur atom forms a fifth ligand for an iron atom in the FTR [4Fe-4S] centre--a unique structure in biology. Fdx then delivers a second electron that cleaves the FTR-Trx heterodisulphide bond, which occurs in the Fdx-FTR-Trx complex. In this structure, the redox centres of the three proteins are aligned to maximize the efficiency of electron transfer from the Fdx [2Fe-2S] cluster to the active-site disulphide of Trxs. These results provide a structural framework for understanding the mechanism of disulphide reduction by an iron-sulphur enzyme and describe previously unknown interaction networks for both Fdx and Trx (refs 4-6)."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.org/dc/terms/identifier"doi:10.1038/nature05937"xsd:string
http://purl.uniprot.org/citations/17611542http://purl.org/dc/terms/identifier"doi:10.1038/nature05937"xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Eklund H."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Eklund H."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Dai S."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Dai S."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Glauser D.A."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Glauser D.A."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Friemann R."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Friemann R."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Bourquin F."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Bourquin F."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Manieri W."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Manieri W."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Schurmann P."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/author"Schurmann P."xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/pages"92-96"xsd:string
http://purl.uniprot.org/citations/17611542http://purl.uniprot.org/core/pages"92-96"xsd:string