The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling
2012
Cejudo Fernández, Francisco Javier | Ferrández, Julia | Cano, Beatriz | Puerto Galán, Leonor | Guinea, Manuel | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | Universidad de Sevilla. BIO182: Biotecnología de Semillas de Cereales | Ministerio de Ciencia e Innovación (MICIN). España | Junta de Andalucía
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.
اظهر المزيد [+] اقل [-]Ministerio de Ciencia e Innovación de España y Fondos FEDER de la Comisión Europea. BIO2010-15430
اظهر المزيد [+] اقل [-]Junta de Andalucía. BIO-182 y CVI-5919
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
المعلومات البيبليوغرافية
تم تزويد هذا السجل من قبل Universidad de Sevilla