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Regulation of NADP-Malate Dehydrogenase Light-Activation by the Reducing Power. I Functional Studies

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Current Research in Photosynthesis

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Abstract

NADP-malate dehydrogenase (MDH) light — activation via the ferredoxin-thioredoxin system requires a low light energy for saturation (1). Nevertheless, high light pretreatments which affect the functionning of photosystem II reaction centers were reported to inhibit enzyme light-activation in crude leaf extracts and in isolated chloroplasts (2,3). In the present work, we investigated the effect of photoinhibitory pretreatments on the different steps of the thiol-disulfide interchange cascade leading to MDH light-activation, in order to establish the relationship between the reduction state of the proteins of the system and the extent of activation of the target enzyme. For that purpose, a model system has been used, composed of isolated thylakoids and all the purified proteins of the ferredoxin-thioredoxin system at optimized concentrations.

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References

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Author information

Authors and Affiliations

  1. Laboratoire de Physiologie Végétale Moléculaire, URA 1128, Université de Paris-Sud, Bât. 430, 91405, Orsay, France

    M. Miginiac-Maslow, P. Decottignies, J.-P. Jacquot & P. Gadal

Authors
  1. M. Miginiac-Maslow
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  2. P. Decottignies
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  3. J.-P. Jacquot
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  4. P. Gadal
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Stockholm, Stockholm, Sweden

    M. Baltscheffsky

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© 1990 Springer Science+Business Media New York

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Miginiac-Maslow, M., Decottignies, P., Jacquot, JP., Gadal, P. (1990). Regulation of NADP-Malate Dehydrogenase Light-Activation by the Reducing Power. I Functional Studies. In: Baltscheffsky, M. (eds) Current Research in Photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0511-5_685

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  • DOI: https://doi.org/10.1007/978-94-009-0511-5_685

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6716-4

  • Online ISBN: 978-94-009-0511-5

  • eBook Packages: Springer Book Archive

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