Recombinant stromal APX defective in the unique loop region showed improved tolerance to hydrogen peroxide

Bioscience, Biotechnology, and Biochemistry
Sakihito KitajimaMasahito Kitamura

Abstract

Ascorbate peroxidase (APX) of chloroplasts plays a pivotal role in detoxifying the hydrogen peroxide (H2O2) produced through photoexcitation of the photosystem, but it easily loses its catalytic activity under attack by excess H2O2. Here we report that the H2O2-tolerance of APX localized in the stroma of chloroplasts was improved by removing a unique 16-amino-acid-residue loop not found in H2O2-tolerant isoforms of cytosol and glyoxysome.

References

Mar 12, 2004·Annual Review of Plant Physiology and Plant Molecular Biology·Kozi Asada
Jun 10, 2008·Biochemical and Biophysical Research Communications·Sakihito KitajimaNamiko Koja

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Citations

Sep 18, 2018·The New Phytologist·Nicholas Smirnoff, Dominique Arnaud
Jul 1, 2017·Nature Communications·Marino Exposito-RodriguezPhilip M Mullineaux
Feb 8, 2018·Free Radical Biology & Medicine·Philip M MullineauxNicholas Smirnoff

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