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Updated: Aug 10, 2026

In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
Published on: October 10, 2014
The 33 kDa protein of photosystem II is a low-affinity calcium- and lanthanide-binding protein
Jerzy Kruk1, Kvetoslava Burda, Małgorzata Jemioła-Rzemińska
1Department of Plant Physiology and Biochemistry, Faculty of Biotechnology, Jagiellonian University, ul. Gronostajowa 7, 30-387 Kraków, Poland. jkruk@mol.uj.edu.pl
Abstract:
We have shown that the isolated 33 kDa protein of photosystem II contains one calcium and one lanthanide low-affinity binding site with binding constants (K(D)) on the order of 10(-5) M. Binding of calcium or lanthanides to this site induces conformational changes in the protein that manifest in fluorescence emission spectra of the protein, circular dichroism spectra, and calorimetric thermograms where the phase transitions are shifted to lower temperatures. The role of calcium binding to the 33 kDa protein in the attainment of its native structure and the significance of this interaction for the oxygen evolution process are discussed.
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