The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling

Cejudo Fernández, Francisco Javier; Ferrández, Julia; Cano, Beatriz; Puerto Galán, Leonor; Guinea, Manuel

doi:10.1016/j.febslet.2012.07.003

Artículo

dc.creator	Cejudo Fernández, Francisco Javier	es
dc.creator	Ferrández, Julia	es
dc.creator	Cano, Beatriz	es
dc.creator	Puerto Galán, Leonor	es
dc.creator	Guinea, Manuel	es
dc.date.accessioned	2022-03-15T10:36:44Z
dc.date.available	2022-03-15T10:36:44Z
dc.date.issued	2012
dc.identifier.citation	Cejudo Fernández, F.J., Ferrández, J., Cano, B., Puerto Galán, L. y Guinea, M. (2012). The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling. FEBS Letters, 586 (18), 2974-2980.
dc.identifier.issn	0014-5793	es
dc.identifier.issn	1873-3468	es
dc.identifier.uri	https://hdl.handle.net/11441/130808
dc.description.abstract	Protein disulphide–dithiol interchange is a universal mechanism of redox regulation in which thioredoxins (Trxs) play an essential role. In heterotrophic organisms, and non-photosynthetic plant organs, NADPH provides the required reducing power in a reaction catalysed by NADPH-dependent thioredoxin reductase (NTR). It has been considered that chloroplasts constitute an exception because reducing equivalents for redox regulation in this organelle is provided by ferredoxin (Fd) reduced by the photosynthetic electron transport chain, not by NADPH. This view was modified by the discovery of a chloroplast-localised NTR, denoted NTRC, a bimodular enzyme formed by NTR and Trx domains with high affinity for NADPH. In this review, we will summarize the present knowledge of the biochemical properties of NTRC and discuss the implications of this enzyme on plastid redox regulation in plants.	es
dc.description.sponsorship	Ministerio de Ciencia e Innovación de España y Fondos FEDER de la Comisión Europea. BIO2010-15430	es
dc.description.sponsorship	Junta de Andalucía. BIO-182 y CVI-5919	es
dc.format	application/pdf	es
dc.format.extent	7 p.	es
dc.language.iso	eng	es
dc.publisher	Elsevier	es
dc.relation.ispartof	FEBS Letters, 586 (18), 2974-2980.
dc.rights	Attribution-NonCommercial-NoDerivatives 4.0 Internacional	*
dc.rights.uri	http://creativecommons.org/licenses/by-nc-nd/4.0/	*
dc.subject	Chloroplast	es
dc.subject	Peroxiredoxin	es
dc.subject	Redox regulation	es
dc.subject	Thioredoxin	es
dc.subject	Thioredoxin reductase	es
dc.title	The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling	es
dc.type	info:eu-repo/semantics/article	es
dcterms.identifier	https://ror.org/03yxnpp24
dc.type.version	info:eu-repo/semantics/publishedVersion	es
dc.rights.accessRights	info:eu-repo/semantics/openAccess	es
dc.contributor.affiliation	Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular	es
dc.relation.projectID	BIO2010-15430	es
dc.relation.projectID	BIO-182	es
dc.relation.projectID	CVI-5919	es
dc.relation.publisherversion	https://doi.org/10.1016/j.febslet.2012.07.003	es
dc.identifier.doi	10.1016/j.febslet.2012.07.003	es
dc.contributor.group	Universidad de Sevilla. BIO182: Biotecnología de Semillas de Cereales	es
dc.journaltitle	FEBS Letters	es
dc.publication.volumen	586	es
dc.publication.issue	18	es
dc.publication.initialPage	2974	es
dc.publication.endPage	2980	es
dc.contributor.funder	Ministerio de Ciencia e Innovación (MICIN). España	es
dc.contributor.funder	Junta de Andalucía	es

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