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

AutorBuey, Ruben M.; Galindo-Trigo, Sergio; López-Maury, Luis ; Velázquez-Campoy, Adrián; Revuelta Doval, José Luis; Florencio, Francisco J.; Pereda, José M. de ; Schürmann, Peter; Buchanan, Bob B.; Balsera, Mónica
Fecha de publicación2017
EditorElsevier
CitaciónMolecular Plant 10(1): 212-215 (2017)
ResumenThioredoxins (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.
Versión del editorhttps://doi.org/10.1016/j.molp.2016.06.019
URIhttp://hdl.handle.net/10261/147131
Identificadoresdoi: 10.1016/j.molp.2016.06.019
issn: 1752-9867
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