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Redox-Modification of Chloroplast Enzymes in Galdieria Sulphuraria: Trial-and-Error in Evolution or Perfect Adaptation to Extreme Conditions?

  • Nicolas König
  • Renate Scheibe
Chapter
Part of the Cellular Origin, Life in Extreme Habitats and Astrobiology book series (COLE, volume 13)

Abstract

Regulation of enzyme activities is required for metabolism, in particular for assimilatory pathways in plastids of all photosynthetic eukaryotic organisms as well as in prokaryotes performing oxygenic photosynthesis. In order to be able to adjust the metabolic fluxes to the actual energy input and the demand, various enzymes have developed structures that are suitable for post-translational regulation by covalent redox-modification (Dietz et al., 2002). Reversible reduction/oxidation of cysteine residues is extremely suited for this purpose. It is mediated by thioredoxins that are present in all organisms (for review see: Buchanan, 1980)

Keywords

Oxygenic Photosynthesis RubisCO Activase CP12 Protein Chloroplast Enzyme Regulatory Cysteine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Notes

Acknowledgments

The authors wish to thank Heike Schwiderski for the preparation of the manuscript. Some of the work described in this paper has been financially supported by the Deutsche Forschungsgemeinschaft.

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Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Department of Plant PhysiologyUniversity of OsnabrueckOsnabrueckGermany

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