Artículo
The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling
Autor/es | Cejudo Fernández, Francisco Javier
Ferrández, Julia Cano, Beatriz Puerto Galán, Leonor Guinea, Manuel |
Departamento | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular |
Fecha de publicación | 2012 |
Fecha de depósito | 2022-03-15 |
Publicado en |
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Resumen | 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 ... 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. |
Agencias financiadoras | Ministerio de Ciencia e Innovación (MICIN). España Junta de Andalucía |
Identificador del proyecto | BIO2010-15430
BIO-182 CVI-5919 |
Cita | 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. |
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