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NTRC new ways of using NADPH in the chloroplast
- Source :
- Physiologia Plantarum. 133:516-524
- Publication Year :
- 2008
- Publisher :
- Wiley, 2008.
-
Abstract
- Despite being the primary source of energy in the biosphere, photosynthesis is a process that inevitably produces reactive oxygen species. Chloroplasts are a major source of hydrogen peroxide production in plant cells; therefore, different systems for peroxide reduction, such as ascorbate peroxidase and peroxiredoxins (Prxs), are found in this organelle. Most of the reducing power required for hydrogen peroxide reduction by these systems is provided by Fd reduced by the photosynthetic electron transport chain; hence, the function of these systems is highly dependent on light. Recently, it was described a novel plastidial enzyme, stated NTRC, formed by a thioredoxin reductase (NTR) domain at the N-terminus and a thioredoxin (Trx) domain at the C-terminus. NTRC is able to conjugate both NTR and Trx activities to efficiently reduce 2-Cys Prx using NADPH as a source of reducing power. Based on these results, it was proposed that NTRC is a new pathway to transfer reducing power to the chloroplast detoxification system, allowing the use of NADPH, besides reduced Fd, for such function. In this article, the most important features of NTRC are summarized and the implications of this novel activity in the context of chloroplast protection against oxidative damage are discussed.
- Subjects :
- Chloroplasts
Physiology
Thioredoxin reductase
Context (language use)
Plant Science
Photosynthesis
Models, Biological
chemistry.chemical_compound
Thioredoxins
Genetics
Hydrogen peroxide
Phylogeny
Plant Proteins
chemistry.chemical_classification
Reactive oxygen species
Binding Sites
biology
Hydrogen Peroxide
Cell Biology
General Medicine
Plants
Chloroplast
Biochemistry
chemistry
biology.protein
Thioredoxin
NADP
Peroxidase
Subjects
Details
- ISSN :
- 13993054 and 00319317
- Volume :
- 133
- Database :
- OpenAIRE
- Journal :
- Physiologia Plantarum
- Accession number :
- edsair.doi.dedup.....2a92823ed1b6cfc6b26aea934d6b0616
- Full Text :
- https://doi.org/10.1111/j.1399-3054.2008.01088.x