The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling
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...
| Autores: | , , , , |
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| Tipo de documento: | artigo |
| Estado: | Versão publicada |
| Data de publicação: | 2012 |
| País: | España |
| Recursos: | Universidad de Sevilla (US) |
| Repositório: | idUS. Depósito de Investigación de la Universidad de Sevilla |
| OAI Identifier: | oai:idus.us.es:11441/130808 |
| Acesso em linha: | https://hdl.handle.net/11441/130808 https://doi.org/10.1016/j.febslet.2012.07.003 |
| Access Level: | Acceso aberto |
| Palavra-chave: | Chloroplast Peroxiredoxin Redox regulation Thioredoxin Thioredoxin reductase |
| Resumo: | 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. |
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