The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling

被引：61

作者：

Javier Cejudo, Francisco ^{[1
]}

Ferrandez, Julia

Cano, Beatriz

Puerto-Galan, Leonor

Guinea, Manuel

机构：

[1] Univ Seville, Inst Bioquim Vegetal & Fotosintesis, Seville 41092, Spain

来源：

FEBS LETTERS | 2012年 / 586卷 / 18期

关键词：

Chloroplast; Peroxiredoxin; Redox regulation; Thioredoxin; Thioredoxin reductase; CYSTEINE-SULFINIC ACID; ADP-GLUCOSE PYROPHOSPHORYLASE; 2-CYSTEINE PEROXIREDOXIN; MAGNESIUM CHELATASE; CHLOROPHYLL BIOSYNTHESIS; OXIDATIVE STRESS; ARABIDOPSIS; CHLOROPLAST; STARCH; NTRC;

D O I：

10.1016/j.febslet.2012.07.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：2974 / 2980

页数：7

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