The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux

König J, Baier M, Horling F, Kahmann U, Harris G, Schurmann P, Dietz K-J (2002)
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 99(8): 5738-5743.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
König, JanineUniBi; Baier, Margarete; Horling, F.; Kahmann, U.; Harris, G.; Schurmann, P.; Dietz, Karl-JosefUniBi
Abstract / Bemerkung
The 2-cysteine peroxiredoxins (2-Cys Prx) constitute an ancient family of peroxide detoxifying enzymes and have acquired a plant-specific function in the oxygenic environment of the chloroplast. Immunocytochemical analysis and work with isolated intact chloroplasts revealed a reversible binding of the oligomeric form of 2-Cys Prx to the thylakoid membrane. The oligomeric form of the enzyme was enhanced under stress. The 2-Cys Prx has a broad substrate specificity with activity toward hydrogen peroxides and complex alkyl hydroperoxides. During the peroxide reduction reaction, 2-Cys Prx is alternatively oxidized and reduced as it catalyzes an electron flow from an electron donor to peroxide. Escherichia coli thioredoxin, but also spinach thioredoxin f and m were able to reduce oxidized 2-Cys Prx. The midpoint redox potential of -315 mV places 2-Cys Prx reduction after Calvin cycle activation and before switching the malate valve for export of excess reduction equivalents to the cytosol. Thus the 2-Cys Prx has a defined and preferential place in the hierarchy of photosynthetic electron transport. The activity of 2-Cys Prx also is linked to chloroplastic NAD(P)H metabolism as indicated by the presence of the reduced form of the enzyme after feeding dihydroxyacetone phosphate to intact chloroplasts. The function of the 2-Cys Prx is therefore not confined to its role in the water-water cycle pathway for energy dissipation in photosynthesis but also mediates peroxide detoxification in the plastids during the dark phase.
Stichworte
Recombinant Proteins/metabolism Substrate Specificity Plastids/metabolism Protein Binding Plant Proteins/metabolism Cell Division Arabidopsis Proteins Chloroplasts/metabolism Electrons Escherichia coli/metabolism Hordeum/physiology Hydrogen Peroxide/metabolism Kinetics Immunohistochemistry Models Biological Mutagenesis Site-Directed *Oxidation-Reduction Oxygen/metabolism Peroxidases/*metabolism/*physiology Peroxides/*metabolism *Photosynthesis Peroxiredoxins Thioredoxins/metabolism Thylakoids/metabolism Time Factors
Erscheinungsjahr
2002
Zeitschriftentitel
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Band
99
Ausgabe
8
Seite(n)
5738-5743
ISSN
0027-8424
eISSN
1091-6490
Page URI
https://pub.uni-bielefeld.de/record/1614655

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König J, Baier M, Horling F, et al. The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2002;99(8):5738-5743.
König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schurmann, P., & Dietz, K. - J. (2002). The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 99(8), 5738-5743. https://doi.org/10.1073/pnas.072644999
König, Janine, Baier, Margarete, Horling, F., Kahmann, U., Harris, G., Schurmann, P., and Dietz, Karl-Josef. 2002. “The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 99 (8): 5738-5743.
König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schurmann, P., and Dietz, K. - J. (2002). The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 99, 5738-5743.
König, J., et al., 2002. The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 99(8), p 5738-5743.
J. König, et al., “The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux”, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 99, 2002, pp. 5738-5743.
König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schurmann, P., Dietz, K.-J.: The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 99, 5738-5743 (2002).
König, Janine, Baier, Margarete, Horling, F., Kahmann, U., Harris, G., Schurmann, P., and Dietz, Karl-Josef. “The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox-hierarchy of photosynthetic electron flux”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 99.8 (2002): 5738-5743.

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