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Title

A new member of the thioredoxin reductase family from early oxygenic photosynthetic organisms

AuthorsMartínez Buey, Rubén CSIC ORCID; Galindo-Trigo, Sergio; López-Maury, Luis CSIC ORCID ; Velázquez-Campoy, Adrián; Revuelta Doval, José Luis CSIC ORCID CVN; Florencio, Francisco J.; Pereda, José M. de CSIC ORCID ; Schürmann, Peter; Buchanan, Bob B.; Balsera, Mónica CSIC ORCID
Issue Date2017
PublisherElsevier
CitationMolecular Plant 10(1): 212-215 (2017)
AbstractThioredoxins (Trxs) are key components of the redox system that regulates the activity of a spectrum of target proteins through dithiol-disulfide exchange reactions. Trxs are reduced by members of the Trx reductase (TR) family (Jacquot et al., 2009). NADP-dependent thioredoxin reductases (NTRs), the most common type, belong to the family of dimeric pyridine nucleotide disulfide oxidoreductase flavoproteins that use NADPH as the source of reducing equivalents. In oxyphotosynthetic organisms, in particular, NTRs coexist with the ferredoxin/thioredoxin system (FTS), composed of ferredoxin (Fdx), ferredoxin:thioredoxin reductase (FTR), and a Trx. FTRs convert the electron signal obtained from photoreduced Fdx to a thiol signal via a 4Fe-4S center and a redox-active disulfide catalytic center. FTR, in turn, reduces Trx.
Publisher version (URL)https://doi.org/10.1016/j.molp.2016.06.019
URIhttp://hdl.handle.net/10261/147131
DOI10.1016/j.molp.2016.06.019
Identifiersdoi: 10.1016/j.molp.2016.06.019
issn: 1752-9867
Appears in Collections:(IBVF) Artículos
(IRNASA) Artículos
(IBMCC) Artículos

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