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Thioredoxin and glutathione regulate photosynthesis in chloroplasts

Naturevolume 266pages565567 (1977) | Download Citation

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Abstract

TWO recently found chloroplast proteins act in the ferredoxin-linked regulation of enzymes of photosynthetic carbon dioxide assimilation1,2. We report here the identification of one of these proteins, earlier termed assimilation regulatory protein b (ARPb), as thioredoxin—a protein functional in the synthesis of DNA and previously not known in chloroplasts3–5. The other protein, assimilation regulatory protein a (ARPa), is a new enzyme that catalyses the reduction of thioredoxin by reduced ferredoxin. We have renamed this protein ‘ferredoxin–thioredoxin reductase.’ In addition to identifying these proteins found earlier, we present evidence for a regulatory function of glutathione in chloroplasts. These findings permit for the first time the formulation of a light-dependent mechanism for protein-mediated enzyme regulation. In this mechanism, key regulatory enzymes are activated (reduced) photochemically via the ferredoxin–thioredoxin system and are deactivated (oxidised) in the dark via oxidised glutathione. The evidence indicates that photoreduced ferredoxin, in the presence of ferredoxin–thioredoxin reductase, controls the level of reduced thioredoxin required for enzyme activation. Glutathione reductase and glutathione peroxidase seem to control the level of oxidised glutathione available for enzyme deactivation.

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  1. Department of Cell Physiology, University of California, Berkeley, California, 94720

    • RICARDO A. WOLOSIUK
    •  & BOB B. BUCHANAN

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https://doi.org/10.1038/266565a0

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