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Photosynth Res. 2019 Nov 25. doi: 10.1007/s11120-019-00691-0. [Epub ahead of print]

Redox regulation by peroxiredoxins is linked to their thioredoxin-dependent oxidase function.

Author information

1
Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 33615, Bielefeld, Germany.
2
Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 33615, Bielefeld, Germany. karl-josef.dietz@uni-bielefeld.de.

Abstract

The chloroplast contains three types of peroxiredoxins (PRXs). Recently, 2-CysPRX was associated with thioredoxin (TRX) oxidation-dependent redox regulation. Here, this analysis was expanded to include PRXQ and PRXIIE. Oxidized PRXQ was able to inactivate NADPH malate dehydrogenase and fructose-1,6-bisphosphatase most efficiently in the presence of TRX-m1 and TRX-m4. The inactivation ability of TRXs did not entirely match their reductive activation efficiency. PRXIIE was unable to function as TRX oxidase in enzyme regulation. This conclusion was further supported by the observation that PRXQ adopts the oxidized form by about 50% in leaves, supporting a possible function as a TRX oxidase similar to 2-CysPRX. Results on the oxidation state of photosystem I (P700), plastocyanin, and ferredoxin in intact leaves indicate that each type of PRX has distinct regulatory functions, and that both 2-CysPRX and PRXQ conditionally assist in adjusting the redox state of target proteins for proper activity.

KEYWORDS:

A. thaliana; Calvin–Benson cycle; Malate valve; Peroxiredoxins; Redox regulation; Thioredoxins

PMID:
31768716
DOI:
10.1007/s11120-019-00691-0

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