Resumen: Thioredoxins (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... Idioma: Inglés DOI: 10.1016/j.molp.2016.06.019 Año: 2017 Publicado en: Molecular Plant 10, 1 (2017), 212-215 ISSN: 1674-2052 Factor impacto JCR: 9.326 (2017) Categ. JCR: PLANT SCIENCES rank: 5 / 222 = 0.023 (2017) - Q1 - T1 Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 16 / 292 = 0.055 (2017) - Q1 - T1 Factor impacto SCIMAGO: 3.562 - Plant Science (Q1) - Molecular Biology (Q1)