Caister Academic Press

Redox Regulation in Chloroplasts

Monica Balsera, Peter Schürmann and Bob B. Buchanan
from: Chloroplasts: Current Research and Future Trends (Edited by: Helmut Kirchhoff). Caister Academic Press, U.K. (2016) Pages: 187-208.

Abstract

The reversible oxidation of cysteine (Cys) residues is commonly used to regulate a range of cellular processes throughout biology. Modification of regulatory Cys alters protein solubility and activity and, under control conditions, ultimately results in the fine-tuning of processes in response to metabolic demands. In oxyphotosynthetic organisms, the reversible modification of protein thiols is a major mechanism for direct regulation of chloroplast enzymes in a light-dependent manner and in response to different types of stress. The main redox regulatory system in chloroplasts is the ferredoxin-dependent thioredoxin system (FTS) which coordinates metabolic pathways of oxygenic photosynthesis via thioredoxin-mediated dithiol/disulfide (SH/S-S) transitions. NADP-linked thioredoxin reductase C and the glutathione/glutaredoxin systems complement the FTS in maintaining redox balance under certain environmental conditions read more ...
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