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Mol Cells. 2016 Jan;39(1):20-5. doi: 10.14348/molcells.2016.2324. Epub 2016 Jan 25.

Thiol-Based Peroxidases and Ascorbate Peroxidases: Why Plants Rely on Multiple Peroxidase Systems in the Photosynthesizing Chloroplast?

Author information

1
Biochemistry and Physiology of Plants, Faculty of Biology, W5-134, Bielefeld University, University Street 25, 33501 Bielefeld, Germany.

Abstract

Photosynthesis is a highly robust process allowing for rapid adjustment to changing environmental conditions. The efficient acclimation depends on balanced redox metabolism and control of reactive oxygen species release which triggers signaling cascades and potentially detrimental oxidation reactions. Thiol peroxidases of the peroxiredoxin and glutathione peroxidase type, and ascorbate peroxidases are the main peroxide detoxifying enzymes of the chloroplast. They use different electron donors and are linked to distinct redox networks. In addition, the peroxiredoxins serve functions in redox regulation and retrograde signaling. The complexity of plastid peroxidases is discussed in context of suborganellar localization, substrate preference, metabolic coupling, protein abundance, activity regulation, interactions, signaling functions, and the conditional requirement for high antioxidant capacity. Thus the review provides an opinion on the advantage of linking detoxification of peroxides to different enzymatic systems and implementing mechanisms for their inactivation to enforce signal propagation within and from the chloroplast.

KEYWORDS:

acorbate peroxidase; chloroplast; peroxiredoxin; photosynthesis; redox sensing

PMID:
26810073
PMCID:
PMC4749869
DOI:
10.14348/molcells.2016.2324
[Indexed for MEDLINE]
Free PMC Article

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